Purification and Characterization of a Recombinant Caulobacter crescentus Epoxide Hydrolase

A Caulobacter crescentus epoxide hydrolase (CCEH) from a recombinant Escherichia coli was purified to homogeneity using a three-step procedure. The CCEH protein was purified 7.3-fold with a 22.9% yield in overall activity. The optimal reaction temperature and pH were determined to be 37℃ and pH 8.0,...

Full description

Saved in:
Bibliographic Details
Published inBiotechnology and bioprocess engineering Vol. 11; no. 4; pp. 282 - 287
Main Authors Hwang, Seungha (Pohang University of Science and Technology, Pohang, Republic of Korea), Hyun, H.J. (Seoul National University, Seoul, Republic of Korea), Lee, B.J. (Seoul National University, Seoul, Republic of Korea), Park, Y.S. (Pohang University of Science and Technology, Pohang, Republic of Korea), Lee, E.Y. (Kyungsung University, Busan, Republic of Korea), Choi, C.Y. (Seoul National University, Seoul, Republic of Korea), E-mail: choicy@snu.ac.kr
Format Journal Article
LanguageEnglish
Published 한국생물공학회 01.08.2006
Subjects
Online AccessGet full text
ISSN1226-8372
1976-3816
DOI10.1007/BF03026241

Cover

Abstract A Caulobacter crescentus epoxide hydrolase (CCEH) from a recombinant Escherichia coli was purified to homogeneity using a three-step procedure. The CCEH protein was purified 7.3-fold with a 22.9% yield in overall activity. The optimal reaction temperature and pH were determined to be 37℃ and pH 8.0, respectively. The addition of 10% (v/v) dimethylsulfoxide as a cosolvent improved the enantioselectivity of CCEH for a batch kinetic resolution of racemic indene oxide.
AbstractList A Caulobacter crescentus epoxide hydrolase (CCEH) from a recombinant Escherichia coli was purified to homogeneity using a three-step procedure. The CCEH protein was purified 7.3-fold with a 22.9% yield in overall activity. The optimal reaction temperature and pH were determined to be 37℃ and pH 8.0, respectively. The addition of 10% (v/v) dimethylsulfoxide as a cosolvent improved the enantioselectivity of CCEH for a batch kinetic resolution of racemic indene oxide.
A Caulobacter crescentus epoxide hydrolase (CCEH) from a recombinant Escherichia coli was purified to homogeneity using a three-step procedure. The CCEH protein was purified 7.3-fold with a 22.9% yield in overall activity. The optimal reaction temperature and pH were determined to be 37oC and pH 8.0, respectively. The addition of 10% (v/v) dimethylsulfoxide as a cosolvent improved the enantioselectivity of CCEH for a batch kinetic resolution of racemic indene oxide. KCI Citation Count: 10
Author Hwang, Seungha (Pohang University of Science and Technology, Pohang, Republic of Korea)
Park, Y.S. (Pohang University of Science and Technology, Pohang, Republic of Korea)
Choi, C.Y. (Seoul National University, Seoul, Republic of Korea), E-mail: choicy@snu.ac.kr
Lee, E.Y. (Kyungsung University, Busan, Republic of Korea)
Hyun, H.J. (Seoul National University, Seoul, Republic of Korea)
Lee, B.J. (Seoul National University, Seoul, Republic of Korea)
Author_xml – sequence: 1
  fullname: Hwang, Seungha (Pohang University of Science and Technology, Pohang, Republic of Korea)
– sequence: 2
  fullname: Hyun, H.J. (Seoul National University, Seoul, Republic of Korea)
– sequence: 3
  fullname: Lee, B.J. (Seoul National University, Seoul, Republic of Korea)
– sequence: 4
  fullname: Park, Y.S. (Pohang University of Science and Technology, Pohang, Republic of Korea)
– sequence: 5
  fullname: Lee, E.Y. (Kyungsung University, Busan, Republic of Korea)
– sequence: 6
  fullname: Choi, C.Y. (Seoul National University, Seoul, Republic of Korea), E-mail: choicy@snu.ac.kr
BackLink https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART001211992$$DAccess content in National Research Foundation of Korea (NRF)
BookMark eNotkEFLAzEUhINUsFYv3oUcvazmJbtJ9liX1hYLSqknD8vbbLbG1kSSLai_3tp6mmH4mIE5JwMfvCXkCtgtMKbu7qdMMC55DidkCKWSmdAgB3vPucy0UPyMnKf0zliutNZD8vq8i65zBnsXPEXf0uoNI5reRvdzDENHkS6tCR-N8-h7WuFuG5oDQ020yVjf7xKdfIYv11o6-25j2GKyF-S0w22yl_86Ii_TyaqaZYunh3k1XmQdB9ZnUliQncG8yIELVYDAtjWlMKWCvCwYAyPbRjDNjGokY2jbQgLTRoumLEGJEbk59vrY1Rvj6oDuoOtQb2I9Xq7mNSj11z4i10e0w1DjOrpUPy75_rn9iihB_ALEv1_K
ContentType Journal Article
DBID FBQ
ACYCR
DOI 10.1007/BF03026241
DatabaseName AGRIS
Korean Citation Index
DatabaseTitleList

Database_xml – sequence: 1
  dbid: FBQ
  name: AGRIS
  url: http://www.fao.org/agris/Centre.asp?Menu_1ID=DB&Menu_2ID=DB1&Language=EN&Content=http://www.fao.org/agris/search?Language=EN
  sourceTypes: Publisher
DeliveryMethod fulltext_linktorsrc
Discipline Engineering
EISSN 1976-3816
EndPage 287
ExternalDocumentID oai_kci_go_kr_ARTI_177412
KR2007001391
GroupedDBID ---
-4Y
-58
-5G
-BR
-EM
-Y2
-~C
.86
.UV
.VR
06C
06D
0R~
0VY
1N0
203
23N
2J2
2JN
2JY
2KG
2KM
2LR
2VQ
2WC
2~H
30V
3V.
4.4
406
408
40D
40E
53G
5GY
5VS
6NX
7WY
7X7
85H
88A
88I
8AO
8FE
8FG
8FH
8FI
8FJ
8FL
8UJ
95-
95.
95~
96X
9ZL
A8Z
AAAVM
AABHQ
AABYN
AAFGU
AAGCJ
AAHNG
AAIAL
AAIKT
AAJKR
AANZL
AARHV
AARTL
AATNV
AATVU
AAUCO
AAUYE
AAWCG
AAYFA
AAYIU
AAYQN
AAYTO
ABDZT
ABECU
ABFGW
ABFTV
ABHQN
ABJCF
ABJNI
ABJOX
ABKAS
ABKCH
ABMNI
ABMQK
ABNWP
ABQBU
ABSXP
ABTEG
ABTHY
ABTKH
ABTMW
ABUWG
ABWNU
ABXPI
ACBMV
ACBRV
ACBXY
ACBYP
ACGFS
ACGOD
ACHSB
ACHXU
ACIGE
ACIPQ
ACIWK
ACKNC
ACMDZ
ACMLO
ACOKC
ACOMO
ACPRK
ACSNA
ACTTH
ACVWB
ACWMK
ADBBV
ADHHG
ADHIR
ADINQ
ADKNI
ADKPE
ADMDM
ADOXG
ADRFC
ADTPH
ADURQ
ADYFF
ADZKW
AEBTG
AEEQQ
AEFTE
AEGAL
AEGNC
AEJHL
AEJRE
AEKMD
AENEX
AEOHA
AEPYU
AESKC
AESTI
AETLH
AEVLU
AEVTX
AEXYK
AFGCZ
AFKRA
AFLOW
AFNRJ
AFQWF
AFRAH
AFWTZ
AFZKB
AGAYW
AGDGC
AGGBP
AGGDS
AGJBK
AGMZJ
AGQMX
AGWIL
AGWZB
AGYKE
AHAVH
AHBYD
AHKAY
AHMBA
AHSBF
AHYZX
AIAKS
AIIXL
AILAN
AIMYW
AITGF
AJBLW
AJDOV
AJGSW
AJRNO
AJZVZ
AKQUC
ALMA_UNASSIGNED_HOLDINGS
ALWAN
AMKLP
AMXSW
AMYLF
AMYQR
AOCGG
ARAPS
ARCSS
ARMRJ
ASPBG
AVWKF
AXYYD
AYJHY
AZFZN
AZQEC
B-.
BA0
BBNVY
BBWZM
BDATZ
BENPR
BEZIV
BGLVJ
BGNMA
BHPHI
BPHCQ
BVXVI
CAG
CCPQU
COF
CS3
CSCUP
DDRTE
DNIVK
DPUIP
DU5
DWQXO
E3Z
EBD
EBLON
EBS
EIOEI
EJD
ESBYG
ESTFP
FBQ
FEDTE
FERAY
FFXSO
FIGPU
FINBP
FNLPD
FRNLG
FRRFC
FSGXE
FWDCC
FYUFA
G-Y
G-Z
GGCAI
GGRSB
GJIRD
GNUQQ
GNWQR
GQ6
GQ7
GROUPED_ABI_INFORM_COMPLETE
HCIFZ
HF~
HG6
HMCUK
HMJXF
HRMNR
HVGLF
HZ~
I-F
IJ-
IKXTQ
IWAJR
IXC
IXD
I~X
I~Z
J-C
J0Z
JBSCW
JZLTJ
K60
K6~
KOV
KVFHK
L6V
LK8
LLZTM
M0C
M0L
M2P
M4Y
M7P
M7S
MA-
ML0
MZR
N2Q
NDZJH
NF0
NPVJJ
NQJWS
NU0
O9-
O93
O9G
O9I
O9J
OK1
P19
P2P
P62
P9N
PF0
PQBIZ
PQQKQ
PROAC
PT4
PT5
PTHSS
Q2X
QOK
QOR
QOS
R89
R9I
RHV
RNI
RNS
ROL
RPX
RSV
RZK
S16
S1Z
S26
S27
S28
S3B
SAP
SCG
SCLPG
SCM
SDH
SHX
SISQX
SNE
SNPRN
SNX
SOHCF
SOJ
SPISZ
SQXTU
SRMVM
SSLCW
STPWE
SZN
T13
T16
TSG
TUC
TUS
U2A
UG4
UKHRP
UNUBA
UOJIU
UTJUX
UZXMN
VC2
VFIZW
W48
W4F
WK8
YLTOR
Z45
Z5O
Z7U
Z7V
Z7W
Z8Q
ZMTXR
ZZE
~A9
AAPBV
ACYCR
ID FETCH-LOGICAL-f210t-63e16fca4541237513addc93c971495001c6db3080c7b600aed56108c83b99173
ISSN 1226-8372
IngestDate Tue Nov 21 21:24:57 EST 2023
Wed Dec 27 19:06:03 EST 2023
IsPeerReviewed true
IsScholarly true
Issue 4
Language English
LinkModel OpenURL
MergedId FETCHMERGED-LOGICAL-f210t-63e16fca4541237513addc93c971495001c6db3080c7b600aed56108c83b99173
Notes E21
2007001391
G704-000785.2006.11.4.001
PageCount 6
ParticipantIDs nrf_kci_oai_kci_go_kr_ARTI_177412
fao_agris_KR2007001391
PublicationCentury 2000
PublicationDate 2006-08-00
PublicationDateYYYYMMDD 2006-08-01
PublicationDate_xml – month: 08
  year: 2006
  text: 2006-08-00
PublicationDecade 2000
PublicationTitle Biotechnology and bioprocess engineering
PublicationYear 2006
Publisher 한국생물공학회
Publisher_xml – name: 한국생물공학회
SSID ssj0047888
Score 1.7531432
Snippet A Caulobacter crescentus epoxide hydrolase (CCEH) from a recombinant Escherichia coli was purified to homogeneity using a three-step procedure. The CCEH...
SourceID nrf
fao
SourceType Open Website
Publisher
StartPage 282
SubjectTerms Caulobacter crescentus
chiral indene oxide
chiral styrene oxide
COMPOSE EPOXY
COMPUESTOS EPOXY
enzyme purification
epoxide hydrolase
EPOXY COMPOUNDS
생물공학
Title Purification and Characterization of a Recombinant Caulobacter crescentus Epoxide Hydrolase
URI https://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART001211992
Volume 11
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
ispartofPNX Biotechnology and Bioprocess Engineering, 2006, 11(4), , pp.282-287
journalDatabaseRights – providerCode: PRVLSH
  databaseName: SpringerLink Journals
  customDbUrl:
  mediaType: online
  eissn: 1976-3816
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0047888
  issn: 1226-8372
  databaseCode: AFBBN
  dateStart: 19961201
  isFulltext: true
  providerName: Library Specific Holdings
– providerCode: PRVPQU
  databaseName: Health & Medical Collection
  customDbUrl:
  eissn: 1976-3816
  dateEnd: 20241102
  omitProxy: true
  ssIdentifier: ssj0047888
  issn: 1226-8372
  databaseCode: 7X7
  dateStart: 19970601
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/healthcomplete
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Central
  customDbUrl: http://www.proquest.com/pqcentral?accountid=15518
  eissn: 1976-3816
  dateEnd: 20241102
  omitProxy: true
  ssIdentifier: ssj0047888
  issn: 1226-8372
  databaseCode: BENPR
  dateStart: 19970601
  isFulltext: true
  titleUrlDefault: https://www.proquest.com/central
  providerName: ProQuest
– providerCode: PRVPQU
  databaseName: ProQuest Technology Collection
  customDbUrl:
  eissn: 1976-3816
  dateEnd: 20241102
  omitProxy: true
  ssIdentifier: ssj0047888
  issn: 1226-8372
  databaseCode: 8FG
  dateStart: 19970601
  isFulltext: true
  titleUrlDefault: https://search.proquest.com/technologycollection1
  providerName: ProQuest
– providerCode: PRVAVX
  databaseName: SpringerLINK - Czech Republic Consortium
  customDbUrl:
  eissn: 1976-3816
  dateEnd: 99991231
  omitProxy: false
  ssIdentifier: ssj0047888
  issn: 1226-8372
  databaseCode: AGYKE
  dateStart: 19970101
  isFulltext: true
  titleUrlDefault: http://link.springer.com
  providerName: Springer Nature
– providerCode: PRVAVX
  databaseName: SpringerLink Journals (ICM)
  customDbUrl:
  eissn: 1976-3816
  dateEnd: 99991231
  omitProxy: true
  ssIdentifier: ssj0047888
  issn: 1226-8372
  databaseCode: U2A
  dateStart: 19970101
  isFulltext: true
  titleUrlDefault: http://www.springerlink.com/journals/
  providerName: Springer Nature
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3da9swEBchfdkexr7Kui80mJ6Ch23JtvQoOynZBmWMFgp7MJJsl1AaFzeBrf_1_oOdZCdRug26vQghny-S79D97nI6IfTeCJaZJuKgvADfGICGQKmGBWDOFVOJgrdcguxJOj9jn86T89Hop5e1tF7pD-b2j-dK_keqMAZytadk_0GyW6YwAH2QL7QgYWjvJeMv685m-vQytBHwYlt--XYLBZWFhu2Vdikvk0KtbQkQSzMBwOhqOa1vJrPr9vuiqifzH1UHzu7NXoJQvmhX2wi8-x29aK_7EwaTelfQcCM8MpsSIYgUZFYQLkku3EhCBN-RFCSHgcJ1QiK57QgJL-1x4YSzodPTyoxw5nMRU5IDSU5ySkTkSCgZ7uv2ohncj2ZspgMcpZ2GnLqZUssMOEmYUv-I2qcDcb8ISXjhbeQAKwNwvvudvu7HAHoF9o9Sf8PmsWf74974_2ZWwl2yfJzGfaWu_drdd2zqXvXuS7MoL9rysivBR_lYRoC47b3YBzEYonCMDuRxnp9s4IO9zsCd39wsYL-m7jABQEKNaqFddo2Hh04fo0eDI4Nlr5VP0KhePkUPvfKWz9A3Xz8x6A2-q5-4bbDCnn5iTz_xTj_xoJ94q5_P0dnx7LSYB8NlHkETR-EqSGkdpY1RLIHF0yyJKFhWI6gRmXXSAS2ZtNIUHBiTaUDhqq4stOeGUw0-TEYP0XjZLusXCBtNdcgaXaeVYIkQqgqpqSKlWRSZKhNH6BA-TqkuwEyWn7_aaLzzdKIj9A6-l5PHX-Xy8h40r9CDne6-RuNVt67fADZd6beDNH8BcQ19qg
linkProvider Library Specific Holdings
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Purification+and+Characterization+of+a+Recombinant+Caulobacter+crescentus+Epoxide+Hydrolase&rft.jtitle=Biotechnology+and+bioprocess+engineering&rft.au=%ED%99%A9%EC%8A%B9%ED%95%98&rft.au=%EC%B5%9C%EC%B0%A8%EC%9A%A9&rft.au=%ED%98%84%ED%98%9C%EC%A7%84&rft.au=%EC%9D%B4%EB%B3%91%EC%A3%BC&rft.date=2006-08-01&rft.pub=%ED%95%9C%EA%B5%AD%EC%83%9D%EB%AC%BC%EA%B3%B5%ED%95%99%ED%9A%8C&rft.issn=1226-8372&rft.eissn=1976-3816&rft.spage=282&rft.epage=287&rft_id=info:doi/10.1007%2FBF03026241&rft.externalDBID=n%2Fa&rft.externalDocID=oai_kci_go_kr_ARTI_177412
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1226-8372&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1226-8372&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1226-8372&client=summon