Bio-enzymes for inhibition and elimination of Escherichia coli O157:H7 biofilm and their synergistic effect with sodium hypochlorite

Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase were evaluated for inhibitory or degrading activity against E. coli O157:H7 biofilm by targeting extracellular DNA, proteins, and cellulose,...

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Published inScientific reports Vol. 9; no. 1; pp. 9920 - 10
Main Authors Lim, Eun Seob, Koo, Ok Kyung, Kim, Min-Jeong, Kim, Joo-Sung
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 09.07.2019
Nature Publishing Group
Subjects
14/19
14/28
14/34
631/326/421
631/326/46
Biodegradation
Biofilms
Biofilms - drug effects
Biofilms - growth & development
Cell number
Cellulase
Cellulase - metabolism
Cellulose
Deoxyribonuclease
Deoxyribonuclease I - metabolism
Drug Synergism
E coli
Endopeptidase K
Endopeptidase K - metabolism
Enzymes
Escherichia coli
Escherichia coli O157 - drug effects
Escherichia coli O157 - growth & development
Escherichia coli O157 - metabolism
Humanities and Social Sciences
Inactivation
multidisciplinary
Oxidants - pharmacology
Proteinase
Science
Science (multidisciplinary)
Sodium
Sodium hypochlorite
Sodium Hypochlorite - pharmacology
Synergistic effect
Online AccessGet full text
ISSN2045-2322
2045-2322
DOI10.1038/s41598-019-46363-w

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Abstract Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase were evaluated for inhibitory or degrading activity against E. coli O157:H7 biofilm by targeting extracellular DNA, proteins, and cellulose, respectively. The cell number of biofilms formed under proteinase K resulted in a 2.43 log CFU/cm 2 reduction with an additional synergistic 3.72 log CFU/cm 2 reduction after NaClO post-treatment, while no significant reduction occurred with NaClO treatment alone. It suggests that protein degradation could be a good way to control the biofilm effectively. In preformed biofilms, all enzymes showed a significant reduction of 16.4–36.7% in biofilm matrix in 10-fold diluted media ( p  < 0.05). The sequential treatment with proteinase K, cellulase, and NaClO showed a significantly higher synergistic inactivation of 2.83 log CFU/cm 2 compared to 1.58 log CFU/cm 2 in the sequence of cellulase, proteinase K, and NaClO ( p  < 0.05). It suggests that the sequence of multiple enzymes can make a significant difference in the susceptibility of biofilms to NaClO. This study indicates that the combination of extracellular polymeric substance-degrading enzymes with NaClO could be useful for the efficient control of E. coli O157:H7 biofilms.
AbstractList Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase were evaluated for inhibitory or degrading activity against E. coli O157:H7 biofilm by targeting extracellular DNA, proteins, and cellulose, respectively. The cell number of biofilms formed under proteinase K resulted in a 2.43 log CFU/cm reduction with an additional synergistic 3.72 log CFU/cm reduction after NaClO post-treatment, while no significant reduction occurred with NaClO treatment alone. It suggests that protein degradation could be a good way to control the biofilm effectively. In preformed biofilms, all enzymes showed a significant reduction of 16.4-36.7% in biofilm matrix in 10-fold diluted media (p < 0.05). The sequential treatment with proteinase K, cellulase, and NaClO showed a significantly higher synergistic inactivation of 2.83 log CFU/cm compared to 1.58 log CFU/cm in the sequence of cellulase, proteinase K, and NaClO (p < 0.05). It suggests that the sequence of multiple enzymes can make a significant difference in the susceptibility of biofilms to NaClO. This study indicates that the combination of extracellular polymeric substance-degrading enzymes with NaClO could be useful for the efficient control of E. coli O157:H7 biofilms.
Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase were evaluated for inhibitory or degrading activity against E. coli O157:H7 biofilm by targeting extracellular DNA, proteins, and cellulose, respectively. The cell number of biofilms formed under proteinase K resulted in a 2.43 log CFU/cm2 reduction with an additional synergistic 3.72 log CFU/cm2 reduction after NaClO post-treatment, while no significant reduction occurred with NaClO treatment alone. It suggests that protein degradation could be a good way to control the biofilm effectively. In preformed biofilms, all enzymes showed a significant reduction of 16.4–36.7% in biofilm matrix in 10-fold diluted media (p < 0.05). The sequential treatment with proteinase K, cellulase, and NaClO showed a significantly higher synergistic inactivation of 2.83 log CFU/cm2 compared to 1.58 log CFU/cm2 in the sequence of cellulase, proteinase K, and NaClO (p < 0.05). It suggests that the sequence of multiple enzymes can make a significant difference in the susceptibility of biofilms to NaClO. This study indicates that the combination of extracellular polymeric substance-degrading enzymes with NaClO could be useful for the efficient control of E. coli O157:H7 biofilms.
Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase were evaluated for inhibitory or degrading activity against E. coli O157:H7 biofilm by targeting extracellular DNA, proteins, and cellulose, respectively. The cell number of biofilms formed under proteinase K resulted in a 2.43 log CFU/cm2 reduction with an additional synergistic 3.72 log CFU/cm2 reduction after NaClO post-treatment, while no significant reduction occurred with NaClO treatment alone. It suggests that protein degradation could be a good way to control the biofilm effectively. In preformed biofilms, all enzymes showed a significant reduction of 16.4-36.7% in biofilm matrix in 10-fold diluted media (p < 0.05). The sequential treatment with proteinase K, cellulase, and NaClO showed a significantly higher synergistic inactivation of 2.83 log CFU/cm2 compared to 1.58 log CFU/cm2 in the sequence of cellulase, proteinase K, and NaClO (p < 0.05). It suggests that the sequence of multiple enzymes can make a significant difference in the susceptibility of biofilms to NaClO. This study indicates that the combination of extracellular polymeric substance-degrading enzymes with NaClO could be useful for the efficient control of E. coli O157:H7 biofilms.Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase were evaluated for inhibitory or degrading activity against E. coli O157:H7 biofilm by targeting extracellular DNA, proteins, and cellulose, respectively. The cell number of biofilms formed under proteinase K resulted in a 2.43 log CFU/cm2 reduction with an additional synergistic 3.72 log CFU/cm2 reduction after NaClO post-treatment, while no significant reduction occurred with NaClO treatment alone. It suggests that protein degradation could be a good way to control the biofilm effectively. In preformed biofilms, all enzymes showed a significant reduction of 16.4-36.7% in biofilm matrix in 10-fold diluted media (p < 0.05). The sequential treatment with proteinase K, cellulase, and NaClO showed a significantly higher synergistic inactivation of 2.83 log CFU/cm2 compared to 1.58 log CFU/cm2 in the sequence of cellulase, proteinase K, and NaClO (p < 0.05). It suggests that the sequence of multiple enzymes can make a significant difference in the susceptibility of biofilms to NaClO. This study indicates that the combination of extracellular polymeric substance-degrading enzymes with NaClO could be useful for the efficient control of E. coli O157:H7 biofilms.
Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase were evaluated for inhibitory or degrading activity against E. coli O157:H7 biofilm by targeting extracellular DNA, proteins, and cellulose, respectively. The cell number of biofilms formed under proteinase K resulted in a 2.43 log CFU/cm 2 reduction with an additional synergistic 3.72 log CFU/cm 2 reduction after NaClO post-treatment, while no significant reduction occurred with NaClO treatment alone. It suggests that protein degradation could be a good way to control the biofilm effectively. In preformed biofilms, all enzymes showed a significant reduction of 16.4–36.7% in biofilm matrix in 10-fold diluted media ( p  < 0.05). The sequential treatment with proteinase K, cellulase, and NaClO showed a significantly higher synergistic inactivation of 2.83 log CFU/cm 2 compared to 1.58 log CFU/cm 2 in the sequence of cellulase, proteinase K, and NaClO ( p  < 0.05). It suggests that the sequence of multiple enzymes can make a significant difference in the susceptibility of biofilms to NaClO. This study indicates that the combination of extracellular polymeric substance-degrading enzymes with NaClO could be useful for the efficient control of E. coli O157:H7 biofilms.
ArticleNumber 9920
Author Lim, Eun Seob
Kim, Joo-Sung
Kim, Min-Jeong
Koo, Ok Kyung
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Cites_doi 10.1046/j.1365-2672.2000.00990.x
10.1007/BF01569989
10.1046/j.1365-2958.2002.02802.x
10.1111/mmi.12994
10.1101/gad.475808
10.1016/S0168-1605(02)00540-8
10.1007/s10482-012-9718-y
10.1099/mic.0.2007/006031-0
10.1128/AEM.02073-07
10.4315/0362-028X-68.3.494
10.1016/j.fm.2015.10.010
10.1089/107662901750152846
10.1371/journal.pone.0015668
10.1128/AEM.69.9.5463-5471.2003
10.1111/jam.12202
10.1089/dna.2009.1011
10.1128/AEM.71.9.5404-5410.2005
10.1094/MPMI-18-0533
10.1111/j.1439-0507.2011.02047.x
10.1016/S0168-1605(98)00060-9
10.1111/1750-3841.12123
10.4315/0362-028X-71.1.66
10.1016/0168-1605(91)90143-D
10.1046/j.1365-2672.2001.01413.x
10.1128/AEM.01065-06
10.1038/nrmicro2415
10.1128/AEM.03109-13
10.18388/abp.2014_1935
10.1002/jsfa.8125
10.1038/mi.2011.27
10.1039/C6FO01201A
10.1016/j.lwt.2016.11.060
10.1073/pnas.1011033108
10.1146/annurev.micro.56.012302.160705
10.4315/0362-028X-68.2.277
10.1094/MPMI-20-9-1083
10.1111/j.1365-2672.2005.02499.x
10.1016/j.lwt.2009.12.008
10.1128/JB.182.12.3593-3596.2000
10.1046/j.1462-2920.2001.00235.x
10.1016/j.lwt.2015.10.049
10.1038/ja.2012.98
10.1016/j.ijfoodmicro.2004.02.014
10.3201/eid0304.970407
10.1016/j.ijfoodmicro.2018.01.014
10.1128/AEM.71.1.247-254.2005
10.1099/mic.0.2008/018093-0
10.1111/j.1365-2621.2008.01839.x
10.1111/1541-4337.12144
10.1038/340301a0
10.1016/0924-2244(96)81255-6
10.1080/19443994.2013.780996
10.3201/eid0505.990502
10.1111/j.1365-2672.2010.04933.x
10.1016/j.ijfoodmicro.2014.06.025
10.4265/bio.11.147
10.1016/S1286-4579(02)01555-1
10.4315/0362-028X-53.7.550
10.1080/08927011003699535
10.4315/0362-028X-66.12.2231
10.1128/JB.00946-13
10.1078/1438-4221-00203
10.1046/j.1432-1327.1998.2510971.x
10.1163/016942411X574961
10.1080/0892701021000030142
10.1111/j.1472-765X.1991.tb00617.x
10.1128/IAI.00219-09
10.1046/j.1365-2672.92.5s1.5.x
10.1111/1758-2229.12085
10.1093/femsre/fuv015
10.3109/1040841X.2013.841639
10.1074/jbc.M109.007054
10.3390/biom8010005
10.1046/j.1365-2958.2001.02337.x
10.4014/jmb.1610.10046
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References Kumar, Anand (CR6) 1998; 42
Nijland, Hall, Burgess (CR41) 2010; 5
Yang (CR81) 2016; 54
Cookson, Cooley, Woodward (CR50) 2002; 292
Mead (CR4) 1999; 5
Okshevsky, Meyer (CR37) 2015; 41
Norwood, Gilmour (CR7) 2000; 88
Pan, Breidt, Kathariou (CR72) 2006; 72
Stoodley, Sauer, Davies, Costerton (CR62) 2002; 56
Cescutti (CR57) 1998; 251
Fouladkhah, Geornaras, Sofos (CR18) 2013; 78
Tetz, Tetz (CR40) 2010; 29
Shukla, Rao (CR46) 2017; 146
Beuchat, Ryu (CR67) 1997; 3
Flemming, Wingender (CR20) 2010; 8
Beuchat (CR3) 2002; 4
Epstein, Pokroy, Seminara, Aizenberg (CR13) 2011; 108
Moryl, Kaleta, Strzelecki, Różalska, Różalski (CR65) 2014; 61
Pawar, Rossman, Chen (CR47) 2005; 99
Qin (CR33) 2007; 153
Fukuzaki (CR68) 2006; 11
Ryu, Beuchat (CR61) 2004; 95
Izano, Amarante, Kher, Kaplan (CR34) 2008; 74
Lim, Lee, Kim, Koo (CR5) 2017; 77
Robbins, Fisher, Moltz, Martin (CR71) 2005; 68
Gilbert, Allison, McBain (CR70) 2002; 92
Devaraj, Justice, Bakaletz, Goodman (CR38) 2015; 96
Bleotu (CR64) 2017; 22
Patel, Sharma, Ravishakar (CR77) 2011; 110
Martins, Henriques, Lopez-Ribot, Oliveira (CR30) 2012; 55
Simões, Simões, Vieira (CR19) 2010; 43
Steinberger, Holden (CR32) 2005; 71
Nur (CR36) 2013; 115
Ryu, Beuchat (CR24) 2005; 71
Biesecker, Nicastro, Wilson, Tükel (CR48) 2018; 8
Czaczyk, Białas, Myszka (CR66) 2008; 57
Weiner, Langille, Quintero (CR21) 1995; 15
Das, Sehar, Manefield (CR31) 2013; 5
Goodman (CR39) 2011; 4
Brooks, Flint (CR12) 2008; 43
Guiton (CR35) 2009; 77
Rajasekharan, Ramesh (CR58) 2013; 62
Doyle (CR1) 1991; 12
Lim, Kim (CR79) 2017; 27
Stewart, Rayner, Roe, Rees (CR8) 2001; 91
Olsén, Jonsson, Normark (CR27) 1989; 340
Cordeiro, Werner (CR78) 2011; 25
Adator, Cheng, Holley, McAllister, Narvaez-Bravo (CR17) 2018; 269
Nguyen, Burrows (CR44) 2014; 187
Corcoran (CR75) 2014; 80
Prakash, Veeregowda, Krishnappa (CR74) 2003; 85
Serra, Richter, Hengge (CR60) 2013; 195
Shewmaker (CR52) 2009; 284
Kusumaningrum, Riboldi, Hazeleger, Beumer (CR14) 2003; 85
Sadekuzzaman, Yang, Mizan, Ha (CR16) 2015; 14
Solano (CR55) 2002; 43
Wadamori, Gooneratne, Hussain (CR2) 2017; 97
Antoniou, Frank (CR23) 2005; 68
Moore, Sheldon, Jaykus (CR15) 2003; 66
Gerstel, Romling (CR54) 2001; 3
Loiselle, Anderson (CR56) 2003; 19
Shukla, Rao (CR45) 2013; 66
Vacheva, Ivanova, Paunova-Krasteva, Stoitsova (CR51) 2012; 102
Pesavento (CR49) 2008; 22
Danese, Pratt, Kolter (CR22) 2000; 182
Kim (CR25) 2013; 51
Wang, Wang, Xing, Wu, Xu (CR43) 2016; 66
Williams, Braun-Howland (CR9) 2003; 69
Sidhu, Langsrud, Holck (CR11) 2001; 7
Zogaj, Nimtz, Rohde, Bokranz, Romling (CR28) 2001; 39
Gualdi (CR59) 2008; 154
Hobley, Harkins, MacPhee, Stanley-Wall (CR29) 2015; 39
Bloomfield, Arthur, Looney, Begun, Patel (CR76) 1991; 13
Barak, Jahn, Gibson, Charkowski (CR53) 2007; 20
Cui, Ma, Lin (CR42) 2016; 7
Laus, van Brussel, Kijne (CR63) 2005; 18
Frank, Koffi (CR69) 1990; 53
Berrang, Frank, Meinersmann (CR73) 2008; 71
Bower, McGuire, Daeschel (CR10) 1996; 7
Lequette, Boels, Clarisse, Faille (CR26) 2010; 26
Elghetany, Saleem, Barr (CR80) 1989; 19
JF Frank (46363_CR69) 1990; 53
LH Kim (46363_CR25) 2013; 51
MC Laus (46363_CR63) 2005; 18
Y Pan (46363_CR72) 2006; 72
EH Adator (46363_CR17) 2018; 269
PN Danese (46363_CR22) 2000; 182
L Gualdi (46363_CR59) 2008; 154
M Loiselle (46363_CR56) 2003; 19
ES Lim (46363_CR79) 2017; 27
PS Guiton (46363_CR35) 2009; 77
UT Nguyen (46363_CR44) 2014; 187
F Shewmaker (46363_CR52) 2009; 284
H Cui (46363_CR42) 2016; 7
CG Kumar (46363_CR6) 1998; 42
A Vacheva (46363_CR51) 2012; 102
A Olsén (46363_CR27) 1989; 340
Z Qin (46363_CR33) 2007; 153
ME Berrang (46363_CR73) 2008; 71
VV Tetz (46363_CR40) 2010; 29
A Fouladkhah (46363_CR18) 2013; 78
R Steinberger (46363_CR32) 2005; 71
C Pesavento (46363_CR49) 2008; 22
P Gilbert (46363_CR70) 2002; 92
AK Epstein (46363_CR13) 2011; 108
P Stoodley (46363_CR62) 2002; 56
Y Wadamori (46363_CR2) 2017; 97
HD Kusumaningrum (46363_CR14) 2003; 85
EA Izano (46363_CR34) 2008; 74
M Moryl (46363_CR65) 2014; 61
C Bleotu (46363_CR64) 2017; 22
DO Serra (46363_CR60) 2013; 195
CK Bower (46363_CR10) 1996; 7
J Patel (46363_CR77) 2011; 110
DE Norwood (46363_CR7) 2000; 88
B Prakash (46363_CR74) 2003; 85
JD Brooks (46363_CR12) 2008; 43
SK Shukla (46363_CR46) 2017; 146
LR Beuchat (46363_CR67) 1997; 3
JB Robbins (46363_CR71) 2005; 68
PS Mead (46363_CR4) 1999; 5
U Gerstel (46363_CR54) 2001; 3
A Devaraj (46363_CR38) 2015; 96
MM Williams (46363_CR9) 2003; 69
H-C Flemming (46363_CR20) 2010; 8
PS Stewart (46363_CR8) 2001; 91
DM Pawar (46363_CR47) 2005; 99
R Weiner (46363_CR21) 1995; 15
M Sadekuzzaman (46363_CR16) 2015; 14
R Nijland (46363_CR41) 2010; 5
L Hobley (46363_CR29) 2015; 39
AL Cordeiro (46363_CR78) 2011; 25
Y Lequette (46363_CR26) 2010; 26
X Zogaj (46363_CR28) 2001; 39
SK Shukla (46363_CR45) 2013; 66
JD Barak (46363_CR53) 2007; 20
M Corcoran (46363_CR75) 2014; 80
SD Goodman (46363_CR39) 2011; 4
LR Beuchat (46363_CR3) 2002; 4
K Antoniou (46363_CR23) 2005; 68
C Solano (46363_CR55) 2002; 43
Y Yang (46363_CR81) 2016; 54
SG Biesecker (46363_CR48) 2018; 8
A Nur (46363_CR36) 2013; 115
J-H Ryu (46363_CR61) 2004; 95
MP Doyle (46363_CR1) 1991; 12
T Das (46363_CR31) 2013; 5
AL Cookson (46363_CR50) 2002; 292
M Simões (46363_CR19) 2010; 43
ES Lim (46363_CR5) 2017; 77
MS Sidhu (46363_CR11) 2001; 7
K Czaczyk (46363_CR66) 2008; 57
M Okshevsky (46363_CR37) 2015; 41
CM Moore (46363_CR15) 2003; 66
S Fukuzaki (46363_CR68) 2006; 11
H Wang (46363_CR43) 2016; 66
M Martins (46363_CR30) 2012; 55
MT Elghetany (46363_CR80) 1989; 19
J-H Ryu (46363_CR24) 2005; 71
SK Rajasekharan (46363_CR58) 2013; 62
P Cescutti (46363_CR57) 1998; 251
SF Bloomfield (46363_CR76) 1991; 13
References_xml – volume: 88
  start-page: 512
  year: 2000
  end-page: 520
  ident: CR7
  article-title: The growth and resistance to sodium hypochlorite of Listeria monocytogenes in a steady-state multispecies biofilm
  publication-title: J. Appl. Microbiol.
  doi: 10.1046/j.1365-2672.2000.00990.x
– volume: 15
  start-page: 339
  year: 1995
  end-page: 346
  ident: CR21
  article-title: Structure, function and immunochemistry of bacterial exopolysaccharides
  publication-title: J. Ind. Microbiol.
  doi: 10.1007/BF01569989
– volume: 43
  start-page: 793
  year: 2002
  end-page: 808
  ident: CR55
  article-title: Genetic analysis of Salmonella Enteritidis biofilm formation: Critical role of cellulose
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2002.02802.x
– volume: 96
  start-page: 1119
  year: 2015
  end-page: 1135
  ident: CR38
  article-title: DNABII proteins play a central role in UPEC biofilm structure
  publication-title: Mol. Microbiol.
  doi: 10.1111/mmi.12994
– volume: 22
  start-page: 2434
  year: 2008
  end-page: 2446
  ident: CR49
  article-title: Inverse regulatory coordination of motility and curli-mediated adhesion in Escherichia coli
  publication-title: Genes Dev.
  doi: 10.1101/gad.475808
– volume: 19
  start-page: 190
  year: 1989
  end-page: 195
  ident: CR80
  article-title: The congo red stain revisited
  publication-title: Ann. Clin. Lab. Sci.
– volume: 85
  start-page: 227
  year: 2003
  end-page: 236
  ident: CR14
  article-title: Survival of foodborne pathogens on stainless steel surfaces and cross-contamination to foods
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/S0168-1605(02)00540-8
– volume: 102
  start-page: 105
  year: 2012
  end-page: 119
  ident: CR51
  article-title: Released products of pathogenic bacteria stimulate biofilm formation by Escherichia coli K-12 strains
  publication-title: Antonie Van Leeuwenhoek
  doi: 10.1007/s10482-012-9718-y
– volume: 153
  start-page: 2083
  year: 2007
  end-page: 2092
  ident: CR33
  article-title: Role of autolysin-mediated DNA release in biofilm formation of Staphylococcus epidermidis
  publication-title: Microbiology
  doi: 10.1099/mic.0.2007/006031-0
– volume: 74
  start-page: 470
  year: 2008
  end-page: 476
  ident: CR34
  article-title: Differential roles of poly-N-acetylglucosamine surface polysaccharide and extracellular DNA in Staphylococcus aureus and Staphylococcus epidermidis biofilms
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.02073-07
– volume: 68
  start-page: 494
  year: 2005
  end-page: 498
  ident: CR71
  article-title: Elimination of Listeria monocytogenes biofilms by ozone, chlorine, and hydrogen peroxide
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-68.3.494
– volume: 54
  start-page: 98
  year: 2016
  end-page: 105
  ident: CR81
  article-title: Biofilm formation of Salmonella Enteritidis under food-related environmental stress conditions and its subsequent resistance to chlorine treatment
  publication-title: Food Microbiol.
  doi: 10.1016/j.fm.2015.10.010
– volume: 7
  start-page: 73
  year: 2001
  end-page: 83
  ident: CR11
  article-title: Disinfectant and antibiotic resistance of lactic acid bacteria isolated from the food industry
  publication-title: Microb. Drug Resist.
  doi: 10.1089/107662901750152846
– volume: 5
  start-page: e15668
  year: 2010
  ident: CR41
  article-title: Dispersal of biofilms by secreted, matrix degrading, bacterial DNase
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0015668
– volume: 69
  start-page: 5463
  year: 2003
  end-page: 5471
  ident: CR9
  article-title: Growth of Escherichia coli in model distribution system biofilms exposed to hypochlorous acid or monochloramine
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.69.9.5463-5471.2003
– volume: 115
  start-page: 260
  year: 2013
  end-page: 270
  ident: CR36
  article-title: Effects of extracellular DNA and DNA-binding protein on the development of a Streptococcus intermedius biofilm
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/jam.12202
– volume: 29
  start-page: 399
  year: 2010
  end-page: 405
  ident: CR40
  article-title: Effect of extracellular DNA destruction by DNase I on characteristics of forming biofilms
  publication-title: DNA Cell Biol.
  doi: 10.1089/dna.2009.1011
– volume: 71
  start-page: 5404
  year: 2005
  end-page: 5410
  ident: CR32
  article-title: Extracellular DNA in single-and multiple-species unsaturated biofilms
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.71.9.5404-5410.2005
– volume: 18
  start-page: 533
  year: 2005
  end-page: 538
  ident: CR63
  article-title: Role of cellulose fibrils and exopolysaccharides of Rhizobium leguminosarum in attachment to and infection of Vicia sativa root hairs
  publication-title: Mol. Plant. Microbe. Interact.
  doi: 10.1094/MPMI-18-0533
– volume: 55
  start-page: 80
  year: 2012
  end-page: 85
  ident: CR30
  article-title: Addition of DNase improves the activity of antifungal drugs against Candida albicans biofilms
  publication-title: Mycoses
  doi: 10.1111/j.1439-0507.2011.02047.x
– volume: 42
  start-page: 9
  year: 1998
  end-page: 27
  ident: CR6
  article-title: Significance of microbial biofilms in food industry: a review
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/S0168-1605(98)00060-9
– volume: 22
  start-page: 12483
  year: 2017
  end-page: 12491
  ident: CR64
  article-title: The influence of nutrient culture media on Escherichia coli adhesion and biofilm formation ability
  publication-title: Rom. Biotechnol. Lett.
– volume: 78
  start-page: M880
  year: 2013
  end-page: M886
  ident: CR18
  article-title: Biofilm formation of O157 and non-O157 shiga toxin-producing Escherichia coli and multidrug-resistant and susceptible Salmonella Typhimurium and Newport and their inactivation by sanitizers
  publication-title: J. Food Sci.
  doi: 10.1111/1750-3841.12123
– volume: 57
  start-page: 313
  year: 2008
  end-page: 319
  ident: CR66
  article-title: Cell surface hydrophobicity of Bacillus spp. as a function of nutrient supply and lipopeptides biosynthesis and its role in adhesion. Polish
  publication-title: J. Microbiol.
– volume: 71
  start-page: 66
  year: 2008
  end-page: 69
  ident: CR73
  article-title: Effect of chemical sanitizers with and without ultrasonication on Listeria monocytogenes as a biofilm within polyvinyl chloride drain pipes
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-71.1.66
– volume: 12
  start-page: 289
  year: 1991
  end-page: 301
  ident: CR1
  article-title: Escherichia coli O157: H7 and its significance in foods
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/0168-1605(91)90143-D
– volume: 91
  start-page: 525
  year: 2001
  end-page: 532
  ident: CR8
  article-title: Biofilm penetration and disinfection efficacy of alkaline hypochlorite and chlorosulfamates
  publication-title: J. Appl. Microbiol.
  doi: 10.1046/j.1365-2672.2001.01413.x
– volume: 72
  start-page: 7711
  year: 2006
  end-page: 7717
  ident: CR72
  article-title: Resistance of Listeria monocytogenes biofilms to sanitizing agents in a simulated food processing environment
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.01065-06
– volume: 8
  start-page: 623
  year: 2010
  end-page: 633
  ident: CR20
  article-title: The biofilm matrix
  publication-title: Nat. Rev. Microbiol.
  doi: 10.1038/nrmicro2415
– volume: 80
  start-page: 1507
  year: 2014
  end-page: 1514
  ident: CR75
  article-title: Commonly used disinfectants fail to eradicate Salmonella enterica biofilms from food contact surface materials
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.03109-13
– volume: 61
  start-page: 133
  year: 2014
  end-page: 139
  ident: CR65
  article-title: Effect of nutrient and stress factors on polysaccharides synthesis in Proteus mirabilis biofilm
  publication-title: Acta Biochim. Pol.
  doi: 10.18388/abp.2014_1935
– volume: 97
  start-page: 1396
  year: 2017
  end-page: 1403
  ident: CR2
  article-title: Outbreaks and factors influencing microbiological contamination of fresh produce
  publication-title: J. Sci. Food Agric.
  doi: 10.1002/jsfa.8125
– volume: 4
  start-page: 625
  year: 2011
  end-page: 637
  ident: CR39
  article-title: Biofilms can be dispersed by focusing the immune system on a common family of bacterial nucleoid-associated proteins
  publication-title: Mucosal Immunol.
  doi: 10.1038/mi.2011.27
– volume: 7
  start-page: 4030
  year: 2016
  end-page: 4040
  ident: CR42
  article-title: Co-loaded proteinase K/thyme oil liposomes for inactivation of Escherichia coli O157:H7 biofilms on cucumber
  publication-title: Food Funct.
  doi: 10.1039/C6FO01201A
– volume: 77
  start-page: 376
  year: 2017
  end-page: 382
  ident: CR5
  article-title: Isolation of indigenous bacteria from a cafeteria kitchen and their biofilm formation and disinfectant susceptibility
  publication-title: LWT - Food Sci. Technol.
  doi: 10.1016/j.lwt.2016.11.060
– volume: 108
  start-page: 995
  year: 2011
  end-page: 1000
  ident: CR13
  article-title: Bacterial biofilm shows persistent resistance to liquid wetting and gas penetration
  publication-title: Proc. Natl. Acad. Sci.
  doi: 10.1073/pnas.1011033108
– volume: 62
  start-page: 327
  year: 2013
  end-page: 330
  ident: CR58
  article-title: Cellulase inhibits Burkholderia cepacia biofilms on diverse prosthetic materials. Polish
  publication-title: J. Microbiol.
– volume: 56
  start-page: 187
  year: 2002
  end-page: 209
  ident: CR62
  article-title: Biofilms as complex differentiated communities
  publication-title: Annu. Rev. Microbiol.
  doi: 10.1146/annurev.micro.56.012302.160705
– volume: 68
  start-page: 277
  year: 2005
  end-page: 281
  ident: CR23
  article-title: Removal of Pseudomonas putida biofilm and associated extracellular polymeric substances from stainless steel by alkali cleaning
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-68.2.277
– volume: 20
  start-page: 1083
  year: 2007
  end-page: 1091
  ident: CR53
  article-title: The role of cellulose and O-antigen capsule in the colonization of plants by Salmonella enterica
  publication-title: Mol. Plant. Microbe. Interact.
  doi: 10.1094/MPMI-20-9-1083
– volume: 99
  start-page: 418
  year: 2005
  end-page: 425
  ident: CR47
  article-title: Role of curli fimbriae in mediating the cells of enterohaemorrhagic Escherichia coli to attach to abiotic surfaces
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/j.1365-2672.2005.02499.x
– volume: 43
  start-page: 573
  year: 2010
  end-page: 583
  ident: CR19
  article-title: A review of current and emergent biofilm control strategies
  publication-title: LWT - Food Sci. Technol.
  doi: 10.1016/j.lwt.2009.12.008
– volume: 182
  start-page: 3593
  year: 2000
  end-page: 3596
  ident: CR22
  article-title: Exopolysaccharide production is required for development of Escherichia coli K-12 biofilm architecture
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.182.12.3593-3596.2000
– volume: 3
  start-page: 638
  year: 2001
  end-page: 648
  ident: CR54
  article-title: Oxygen tension and nutrient starvation are major signals that regulate agfD promoter activity and expression of the multicellular morphotype in Salmonella Typhimurium
  publication-title: Environ. Microbiol.
  doi: 10.1046/j.1462-2920.2001.00235.x
– volume: 27
  start-page: 1609
  year: 2017
  end-page: 1616
  ident: CR79
  article-title: Role of eptC in biofilm formation by Campylobacter jejuni NCTC11168 on polystyrene and glass surfaces
  publication-title: J. Microbiol. Biotechnol.
– volume: 66
  start-page: 298
  year: 2016
  end-page: 304
  ident: CR43
  article-title: Removal of Salmonella biofilm formed under meat processing environment by surfactant in combination with bio-enzyme
  publication-title: LWT - Food Sci. Technol.
  doi: 10.1016/j.lwt.2015.10.049
– volume: 66
  start-page: 55
  year: 2013
  end-page: 60
  ident: CR45
  article-title: Dispersal of Bap-mediated Staphylococcus aureus biofilm by proteinase K
  publication-title: J. Antibiot. (Tokyo).
  doi: 10.1038/ja.2012.98
– volume: 95
  start-page: 189
  year: 2004
  end-page: 204
  ident: CR61
  article-title: Factors affecting production of extracellular carbohydrate complexes by Escherichia coli O157:H7
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/j.ijfoodmicro.2004.02.014
– volume: 3
  start-page: 459
  year: 1997
  end-page: 465
  ident: CR67
  article-title: Produce handling and processing practices
  publication-title: Emerg. Infect. Dis.
  doi: 10.3201/eid0304.970407
– volume: 269
  start-page: 52
  year: 2018
  end-page: 59
  ident: CR17
  article-title: Ability of Shiga toxigenic Escherichia coli to survive within dry-surface biofilms and transfer to fresh lettuce
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/j.ijfoodmicro.2018.01.014
– volume: 71
  start-page: 247
  year: 2005
  end-page: 254
  ident: CR24
  article-title: Biofilm formation by Escherichia coli O157:H7 on stainless steel: effect of exopolysaccharide and curli production on its resistance to chlorine
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.71.1.247-254.2005
– volume: 154
  start-page: 2017
  year: 2008
  end-page: 2024
  ident: CR59
  article-title: Cellulose modulates biofilm formation by counteracting curli-mediated colonization of solid surfaces in Escherichia coli
  publication-title: Microbiology
  doi: 10.1099/mic.0.2008/018093-0
– volume: 43
  start-page: 2163
  year: 2008
  end-page: 2176
  ident: CR12
  article-title: Biofilms in the food industry: problems and potential solutions
  publication-title: Int. J. Food Sci. Technol.
  doi: 10.1111/j.1365-2621.2008.01839.x
– volume: 85
  start-page: 1299
  year: 2003
  end-page: 1307
  ident: CR74
  article-title: Biofilms: A survival strategy of bacteria
  publication-title: Curr. Sci.
– volume: 14
  start-page: 491
  year: 2015
  end-page: 509
  ident: CR16
  article-title: Current and recent advanced strategies for combating biofilms
  publication-title: Compr. Rev. Food Sci. Food Saf.
  doi: 10.1111/1541-4337.12144
– volume: 340
  start-page: 301
  year: 1989
  end-page: 303
  ident: CR27
  article-title: Fibronectin binding mediated by a novel class of surface organelles on Escherichia coli
  publication-title: Nature
  doi: 10.1038/340301a0
– volume: 7
  start-page: 152
  year: 1996
  end-page: 157
  ident: CR10
  article-title: The adhesion and detachment of bacteria and spores on food-contact surfaces
  publication-title: Trends Food Sci. Technol.
  doi: 10.1016/0924-2244(96)81255-6
– volume: 51
  start-page: 6355
  year: 2013
  end-page: 6361
  ident: CR25
  article-title: Effects of enzymatic treatment on the reduction of extracellular polymeric substances (EPS) from biofouled membranes
  publication-title: Desalin. Water Treat.
  doi: 10.1080/19443994.2013.780996
– volume: 5
  start-page: 607
  year: 1999
  end-page: 625
  ident: CR4
  article-title: Food-related illness and death in the United States
  publication-title: Emerg. Infect. Dis.
  doi: 10.3201/eid0505.990502
– volume: 110
  start-page: 737
  year: 2011
  end-page: 745
  ident: CR77
  article-title: Effect of curli expression and hydrophobicity of Escherichia coli O157:H7 on attachment to fresh produce surfaces
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/j.1365-2672.2010.04933.x
– volume: 187
  start-page: 26
  year: 2014
  end-page: 32
  ident: CR44
  article-title: DNase I and proteinase K impair Listeria monocytogenes biofilm formation and induce dispersal of pre-existing biofilms
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/j.ijfoodmicro.2014.06.025
– volume: 11
  start-page: 147
  year: 2006
  end-page: 157
  ident: CR68
  article-title: Mechanisms of actions of sodium hypochlorite in cleaning and disinfection processes
  publication-title: Biocontrol Sci.
  doi: 10.4265/bio.11.147
– volume: 146
  start-page: S1
  year: 2017
  end-page: S8
  ident: CR46
  article-title: Staphylococcus aureus biofilm removal by targeting biofilm-associated extracellular proteins
  publication-title: Indian J. Med. Res.
– volume: 4
  start-page: 413
  year: 2002
  end-page: 423
  ident: CR3
  article-title: Ecological factors influencing survival and growth of human pathogens on raw fruits and vegetables
  publication-title: Microbes Infect.
  doi: 10.1016/S1286-4579(02)01555-1
– volume: 53
  start-page: 550
  year: 1990
  end-page: 554
  ident: CR69
  article-title: Surface-adherent growth of Listeria monocytogenes is associated with increased resistance to surfactant sanitizers and heat
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-53.7.550
– volume: 26
  start-page: 421
  year: 2010
  end-page: 431
  ident: CR26
  article-title: Using enzymes to remove biofilms of bacterial isolates sampled in the food-industry
  publication-title: Biofouling
  doi: 10.1080/08927011003699535
– volume: 66
  start-page: 2231
  year: 2003
  end-page: 2236
  ident: CR15
  article-title: Transfer of Salmonella and Campylobacter from stainless steel to romaine lettuce
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-66.12.2231
– volume: 195
  start-page: 5540
  year: 2013
  end-page: 5554
  ident: CR60
  article-title: Cellulose as an architectural element in spatially structured Escherichia coli biofilms
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.00946-13
– volume: 292
  start-page: 195
  year: 2002
  end-page: 205
  ident: CR50
  article-title: The role of type 1 and curli fimbriae of Shiga toxin-producing Escherichia coli in adherence to abiotic surfaces
  publication-title: Int. J. Med. Microbiol.
  doi: 10.1078/1438-4221-00203
– volume: 251
  start-page: 971
  year: 1998
  end-page: 979
  ident: CR57
  article-title: Structural investigation of the exopolysaccharide produced by Pseudomonas flavescens strain B62–degradation by a fungal cellulase and isolation of the oligosaccharide repeating unit
  publication-title: Eur. J. Biochem.
  doi: 10.1046/j.1432-1327.1998.2510971.x
– volume: 25
  start-page: 2317
  year: 2011
  end-page: 2344
  ident: CR78
  article-title: Enzymes for antifouling strategies
  publication-title: J. Adhes. Sci. Technol.
  doi: 10.1163/016942411X574961
– volume: 19
  start-page: 77
  year: 2003
  end-page: 85
  ident: CR56
  article-title: The use of cellulase in inhibiting biofilm formation from organisms commonly found on medical implants
  publication-title: Biofouling
  doi: 10.1080/0892701021000030142
– volume: 13
  start-page: 233
  year: 1991
  end-page: 237
  ident: CR76
  article-title: Comparative testing of disinfectant and antiseptic products using proposed European suspension testing methods
  publication-title: Lett. Appl. Microbiol.
  doi: 10.1111/j.1472-765X.1991.tb00617.x
– volume: 77
  start-page: 3626
  year: 2009
  end-page: 3638
  ident: CR35
  article-title: Contribution of autolysin and sortase A during Enterococcus faecalis DNA-dependent biofilm development
  publication-title: Infect. Immun.
  doi: 10.1128/IAI.00219-09
– volume: 92
  start-page: 98S
  year: 2002
  end-page: 110S
  ident: CR70
  article-title: Biofilms and : do singular mechanisms imply cross-resistance?
  publication-title: J. Appl. Microbiol.
  doi: 10.1046/j.1365-2672.92.5s1.5.x
– volume: 5
  start-page: 778
  year: 2013
  end-page: 786
  ident: CR31
  article-title: The roles of extracellular DNA in the structural integrity of extracellular polymeric substance and bacterial biofilm development
  publication-title: Environ. Microbiol. Rep.
  doi: 10.1111/1758-2229.12085
– volume: 39
  start-page: 649
  year: 2015
  end-page: 669
  ident: CR29
  article-title: Giving structure to the biofilm matrix: an overview of individual strategies and emerging common themes
  publication-title: FEMS Microbiol. Rev.
  doi: 10.1093/femsre/fuv015
– volume: 41
  start-page: 341
  year: 2015
  end-page: 352
  ident: CR37
  article-title: The role of extracellular DNA in the establishment, maintenance and perpetuation of bacterial biofilms
  publication-title: Crit. Rev. Microbiol.
  doi: 10.3109/1040841X.2013.841639
– volume: 284
  start-page: 25065
  year: 2009
  end-page: 25076
  ident: CR52
  article-title: The functional curli amyloid is not based on in-register parallel β-sheet structure
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M109.007054
– volume: 8
  start-page: 5
  year: 2018
  ident: CR48
  article-title: The functional amyloid curli protects Escherichia coli against complement-mediated bactericidal activity
  publication-title: Biomolecules
  doi: 10.3390/biom8010005
– volume: 39
  start-page: 1452
  year: 2001
  end-page: 1463
  ident: CR28
  article-title: The multicellular morphotypes of Salmonella Typhimurium and Escherichia coli produce cellulose as the second component of the extracellular matrix
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2001.02337.x
– volume: 146
  start-page: S1
  year: 2017
  ident: 46363_CR46
  publication-title: Indian J. Med. Res.
– volume: 14
  start-page: 491
  year: 2015
  ident: 46363_CR16
  publication-title: Compr. Rev. Food Sci. Food Saf.
  doi: 10.1111/1541-4337.12144
– volume: 68
  start-page: 494
  year: 2005
  ident: 46363_CR71
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-68.3.494
– volume: 340
  start-page: 301
  year: 1989
  ident: 46363_CR27
  publication-title: Nature
  doi: 10.1038/340301a0
– volume: 5
  start-page: 778
  year: 2013
  ident: 46363_CR31
  publication-title: Environ. Microbiol. Rep.
  doi: 10.1111/1758-2229.12085
– volume: 7
  start-page: 4030
  year: 2016
  ident: 46363_CR42
  publication-title: Food Funct.
  doi: 10.1039/C6FO01201A
– volume: 92
  start-page: 98S
  year: 2002
  ident: 46363_CR70
  publication-title: J. Appl. Microbiol.
  doi: 10.1046/j.1365-2672.92.5s1.5.x
– volume: 26
  start-page: 421
  year: 2010
  ident: 46363_CR26
  publication-title: Biofouling
  doi: 10.1080/08927011003699535
– volume: 19
  start-page: 190
  year: 1989
  ident: 46363_CR80
  publication-title: Ann. Clin. Lab. Sci.
– volume: 5
  start-page: 607
  year: 1999
  ident: 46363_CR4
  publication-title: Emerg. Infect. Dis.
  doi: 10.3201/eid0505.990502
– volume: 292
  start-page: 195
  year: 2002
  ident: 46363_CR50
  publication-title: Int. J. Med. Microbiol.
  doi: 10.1078/1438-4221-00203
– volume: 25
  start-page: 2317
  year: 2011
  ident: 46363_CR78
  publication-title: J. Adhes. Sci. Technol.
  doi: 10.1163/016942411X574961
– volume: 195
  start-page: 5540
  year: 2013
  ident: 46363_CR60
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.00946-13
– volume: 154
  start-page: 2017
  year: 2008
  ident: 46363_CR59
  publication-title: Microbiology
  doi: 10.1099/mic.0.2008/018093-0
– volume: 68
  start-page: 277
  year: 2005
  ident: 46363_CR23
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-68.2.277
– volume: 53
  start-page: 550
  year: 1990
  ident: 46363_CR69
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-53.7.550
– volume: 27
  start-page: 1609
  year: 2017
  ident: 46363_CR79
  publication-title: J. Microbiol. Biotechnol.
  doi: 10.4014/jmb.1610.10046
– volume: 54
  start-page: 98
  year: 2016
  ident: 46363_CR81
  publication-title: Food Microbiol.
  doi: 10.1016/j.fm.2015.10.010
– volume: 91
  start-page: 525
  year: 2001
  ident: 46363_CR8
  publication-title: J. Appl. Microbiol.
  doi: 10.1046/j.1365-2672.2001.01413.x
– volume: 43
  start-page: 573
  year: 2010
  ident: 46363_CR19
  publication-title: LWT - Food Sci. Technol.
  doi: 10.1016/j.lwt.2009.12.008
– volume: 85
  start-page: 227
  year: 2003
  ident: 46363_CR14
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/S0168-1605(02)00540-8
– volume: 18
  start-page: 533
  year: 2005
  ident: 46363_CR63
  publication-title: Mol. Plant. Microbe. Interact.
  doi: 10.1094/MPMI-18-0533
– volume: 15
  start-page: 339
  year: 1995
  ident: 46363_CR21
  publication-title: J. Ind. Microbiol.
  doi: 10.1007/BF01569989
– volume: 51
  start-page: 6355
  year: 2013
  ident: 46363_CR25
  publication-title: Desalin. Water Treat.
  doi: 10.1080/19443994.2013.780996
– volume: 77
  start-page: 3626
  year: 2009
  ident: 46363_CR35
  publication-title: Infect. Immun.
  doi: 10.1128/IAI.00219-09
– volume: 7
  start-page: 73
  year: 2001
  ident: 46363_CR11
  publication-title: Microb. Drug Resist.
  doi: 10.1089/107662901750152846
– volume: 66
  start-page: 298
  year: 2016
  ident: 46363_CR43
  publication-title: LWT - Food Sci. Technol.
  doi: 10.1016/j.lwt.2015.10.049
– volume: 99
  start-page: 418
  year: 2005
  ident: 46363_CR47
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/j.1365-2672.2005.02499.x
– volume: 284
  start-page: 25065
  year: 2009
  ident: 46363_CR52
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M109.007054
– volume: 115
  start-page: 260
  year: 2013
  ident: 46363_CR36
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/jam.12202
– volume: 66
  start-page: 2231
  year: 2003
  ident: 46363_CR15
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-66.12.2231
– volume: 4
  start-page: 625
  year: 2011
  ident: 46363_CR39
  publication-title: Mucosal Immunol.
  doi: 10.1038/mi.2011.27
– volume: 3
  start-page: 459
  year: 1997
  ident: 46363_CR67
  publication-title: Emerg. Infect. Dis.
  doi: 10.3201/eid0304.970407
– volume: 29
  start-page: 399
  year: 2010
  ident: 46363_CR40
  publication-title: DNA Cell Biol.
  doi: 10.1089/dna.2009.1011
– volume: 12
  start-page: 289
  year: 1991
  ident: 46363_CR1
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/0168-1605(91)90143-D
– volume: 39
  start-page: 649
  year: 2015
  ident: 46363_CR29
  publication-title: FEMS Microbiol. Rev.
  doi: 10.1093/femsre/fuv015
– volume: 20
  start-page: 1083
  year: 2007
  ident: 46363_CR53
  publication-title: Mol. Plant. Microbe. Interact.
  doi: 10.1094/MPMI-20-9-1083
– volume: 39
  start-page: 1452
  year: 2001
  ident: 46363_CR28
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2001.02337.x
– volume: 71
  start-page: 247
  year: 2005
  ident: 46363_CR24
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.71.1.247-254.2005
– volume: 77
  start-page: 376
  year: 2017
  ident: 46363_CR5
  publication-title: LWT - Food Sci. Technol.
  doi: 10.1016/j.lwt.2016.11.060
– volume: 108
  start-page: 995
  year: 2011
  ident: 46363_CR13
  publication-title: Proc. Natl. Acad. Sci.
  doi: 10.1073/pnas.1011033108
– volume: 72
  start-page: 7711
  year: 2006
  ident: 46363_CR72
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.01065-06
– volume: 269
  start-page: 52
  year: 2018
  ident: 46363_CR17
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/j.ijfoodmicro.2018.01.014
– volume: 22
  start-page: 12483
  year: 2017
  ident: 46363_CR64
  publication-title: Rom. Biotechnol. Lett.
– volume: 61
  start-page: 133
  year: 2014
  ident: 46363_CR65
  publication-title: Acta Biochim. Pol.
  doi: 10.18388/abp.2014_1935
– volume: 110
  start-page: 737
  year: 2011
  ident: 46363_CR77
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/j.1365-2672.2010.04933.x
– volume: 57
  start-page: 313
  year: 2008
  ident: 46363_CR66
  publication-title: J. Microbiol.
– volume: 74
  start-page: 470
  year: 2008
  ident: 46363_CR34
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.02073-07
– volume: 7
  start-page: 152
  year: 1996
  ident: 46363_CR10
  publication-title: Trends Food Sci. Technol.
  doi: 10.1016/0924-2244(96)81255-6
– volume: 182
  start-page: 3593
  year: 2000
  ident: 46363_CR22
  publication-title: J. Bacteriol.
  doi: 10.1128/JB.182.12.3593-3596.2000
– volume: 85
  start-page: 1299
  year: 2003
  ident: 46363_CR74
  publication-title: Curr. Sci.
– volume: 56
  start-page: 187
  year: 2002
  ident: 46363_CR62
  publication-title: Annu. Rev. Microbiol.
  doi: 10.1146/annurev.micro.56.012302.160705
– volume: 78
  start-page: M880
  year: 2013
  ident: 46363_CR18
  publication-title: J. Food Sci.
  doi: 10.1111/1750-3841.12123
– volume: 42
  start-page: 9
  year: 1998
  ident: 46363_CR6
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/S0168-1605(98)00060-9
– volume: 8
  start-page: 5
  year: 2018
  ident: 46363_CR48
  publication-title: Biomolecules
  doi: 10.3390/biom8010005
– volume: 43
  start-page: 2163
  year: 2008
  ident: 46363_CR12
  publication-title: Int. J. Food Sci. Technol.
  doi: 10.1111/j.1365-2621.2008.01839.x
– volume: 96
  start-page: 1119
  year: 2015
  ident: 46363_CR38
  publication-title: Mol. Microbiol.
  doi: 10.1111/mmi.12994
– volume: 8
  start-page: 623
  year: 2010
  ident: 46363_CR20
  publication-title: Nat. Rev. Microbiol.
  doi: 10.1038/nrmicro2415
– volume: 5
  start-page: e15668
  year: 2010
  ident: 46363_CR41
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0015668
– volume: 71
  start-page: 66
  year: 2008
  ident: 46363_CR73
  publication-title: J. Food Prot.
  doi: 10.4315/0362-028X-71.1.66
– volume: 3
  start-page: 638
  year: 2001
  ident: 46363_CR54
  publication-title: Environ. Microbiol.
  doi: 10.1046/j.1462-2920.2001.00235.x
– volume: 11
  start-page: 147
  year: 2006
  ident: 46363_CR68
  publication-title: Biocontrol Sci.
  doi: 10.4265/bio.11.147
– volume: 69
  start-page: 5463
  year: 2003
  ident: 46363_CR9
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.69.9.5463-5471.2003
– volume: 80
  start-page: 1507
  year: 2014
  ident: 46363_CR75
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.03109-13
– volume: 4
  start-page: 413
  year: 2002
  ident: 46363_CR3
  publication-title: Microbes Infect.
  doi: 10.1016/S1286-4579(02)01555-1
– volume: 19
  start-page: 77
  year: 2003
  ident: 46363_CR56
  publication-title: Biofouling
  doi: 10.1080/0892701021000030142
– volume: 71
  start-page: 5404
  year: 2005
  ident: 46363_CR32
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.71.9.5404-5410.2005
– volume: 22
  start-page: 2434
  year: 2008
  ident: 46363_CR49
  publication-title: Genes Dev.
  doi: 10.1101/gad.475808
– volume: 43
  start-page: 793
  year: 2002
  ident: 46363_CR55
  publication-title: Mol. Microbiol.
  doi: 10.1046/j.1365-2958.2002.02802.x
– volume: 187
  start-page: 26
  year: 2014
  ident: 46363_CR44
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/j.ijfoodmicro.2014.06.025
– volume: 66
  start-page: 55
  year: 2013
  ident: 46363_CR45
  publication-title: J. Antibiot. (Tokyo).
  doi: 10.1038/ja.2012.98
– volume: 251
  start-page: 971
  year: 1998
  ident: 46363_CR57
  publication-title: Eur. J. Biochem.
  doi: 10.1046/j.1432-1327.1998.2510971.x
– volume: 62
  start-page: 327
  year: 2013
  ident: 46363_CR58
  publication-title: J. Microbiol.
– volume: 95
  start-page: 189
  year: 2004
  ident: 46363_CR61
  publication-title: Int. J. Food Microbiol.
  doi: 10.1016/j.ijfoodmicro.2004.02.014
– volume: 97
  start-page: 1396
  year: 2017
  ident: 46363_CR2
  publication-title: J. Sci. Food Agric.
  doi: 10.1002/jsfa.8125
– volume: 13
  start-page: 233
  year: 1991
  ident: 46363_CR76
  publication-title: Lett. Appl. Microbiol.
  doi: 10.1111/j.1472-765X.1991.tb00617.x
– volume: 153
  start-page: 2083
  year: 2007
  ident: 46363_CR33
  publication-title: Microbiology
  doi: 10.1099/mic.0.2007/006031-0
– volume: 88
  start-page: 512
  year: 2000
  ident: 46363_CR7
  publication-title: J. Appl. Microbiol.
  doi: 10.1046/j.1365-2672.2000.00990.x
– volume: 55
  start-page: 80
  year: 2012
  ident: 46363_CR30
  publication-title: Mycoses
  doi: 10.1111/j.1439-0507.2011.02047.x
– volume: 41
  start-page: 341
  year: 2015
  ident: 46363_CR37
  publication-title: Crit. Rev. Microbiol.
  doi: 10.3109/1040841X.2013.841639
– volume: 102
  start-page: 105
  year: 2012
  ident: 46363_CR51
  publication-title: Antonie Van Leeuwenhoek
  doi: 10.1007/s10482-012-9718-y
SSID ssj0000529419
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Snippet Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase...
Escherichia coli O157:H7 is one of the most important pathogens worldwide. In this study, three different kinds of enzymes, DNase I, proteinase K and cellulase...
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StartPage 9920
SubjectTerms 14/19
14/28
14/34
631/326/421
631/326/46
Biodegradation
Biofilms
Biofilms - drug effects
Biofilms - growth & development
Cell number
Cellulase
Cellulase - metabolism
Cellulose
Deoxyribonuclease
Deoxyribonuclease I - metabolism
Drug Synergism
E coli
Endopeptidase K
Endopeptidase K - metabolism
Enzymes
Escherichia coli
Escherichia coli O157 - drug effects
Escherichia coli O157 - growth & development
Escherichia coli O157 - metabolism
Humanities and Social Sciences
Inactivation
multidisciplinary
Oxidants - pharmacology
Proteinase
Science
Science (multidisciplinary)
Sodium
Sodium hypochlorite
Sodium Hypochlorite - pharmacology
Synergistic effect
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Title Bio-enzymes for inhibition and elimination of Escherichia coli O157:H7 biofilm and their synergistic effect with sodium hypochlorite
URI https://link.springer.com/article/10.1038/s41598-019-46363-w
https://www.ncbi.nlm.nih.gov/pubmed/31289312
https://www.proquest.com/docview/2254473221
https://www.proquest.com/docview/2255473222
https://pubmed.ncbi.nlm.nih.gov/PMC6616338
Volume 9
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