Properties of a novel polydatin-β-d-glucosidase from Aspergillus niger SK34.002 and its application in enzymatic preparation of resveratrol
BACKGROUND Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum. Resveratrol has become the subject of intensive research over the past two decades owing to its outstanding pharmacological properties. However, its lower concentration in plants compared to polydatin...
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| Published in | Journal of the science of food and agriculture Vol. 96; no. 7; pp. 2588 - 2595 |
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| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Chichester, UK
John Wiley & Sons, Ltd
01.05.2016
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| Subjects | |
| Online Access | Get full text |
| ISSN | 0022-5142 1097-0010 |
| DOI | 10.1002/jsfa.7465 |
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| Abstract | BACKGROUND
Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum. Resveratrol has become the subject of intensive research over the past two decades owing to its outstanding pharmacological properties. However, its lower concentration in plants compared to polydatin limits its application. In this study, the polydatin‐β‐d‐glucosidase (PBG) that hydrolyzes the β‐d‐glucosyl residue of polydatin with release of resveratrol was purified to homogeneity and characterized.
RESULTS
The molecular weight of PBG was estimated to be 125 kDa by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and 128 kDa by size‐exclusion chromatography– multi‐angle laser light scattering/ultraviolet/refractive index. The optimal PBG activity was observed at 70 °C and pH 4.5. The enzyme showed around 50% stability at 60 °C for 12 h and residual activity was over 80% at pH 3.0–5.0. Ca2+, Mg2+, Mn2+, Zn2+, Ba2+, Ni2+, Co2+ and Cu2+ ions had no significant effect on the enzyme activity. The PBG presented higher affinity to polydatin (Km = 0.74 mmol L−1) than p‐nitrophenyl‐β‐d‐glucopyranoside (Km = 2.9 mmol L−1) and cellobiose (Km = 8.9 mmol L−1).
CONCLUSION
With this enzyme, nearly all polydatin in P. cuspidatum was converted to resveratrol. Although several β‐D‐glucosidases (BGLs) have been obtained from other sources, PBG is distinguished from other BGLs by its outstanding thermal stability and high catalytic efficiency. © 2015 Society of Chemical Industry |
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| AbstractList | BACKGROUND
Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum. Resveratrol has become the subject of intensive research over the past two decades owing to its outstanding pharmacological properties. However, its lower concentration in plants compared to polydatin limits its application. In this study, the polydatin‐β‐d‐glucosidase (PBG) that hydrolyzes the β‐d‐glucosyl residue of polydatin with release of resveratrol was purified to homogeneity and characterized.
RESULTS
The molecular weight of PBG was estimated to be 125 kDa by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and 128 kDa by size‐exclusion chromatography– multi‐angle laser light scattering/ultraviolet/refractive index. The optimal PBG activity was observed at 70 °C and pH 4.5. The enzyme showed around 50% stability at 60 °C for 12 h and residual activity was over 80% at pH 3.0–5.0. Ca2+, Mg2+, Mn2+, Zn2+, Ba2+, Ni2+, Co2+ and Cu2+ ions had no significant effect on the enzyme activity. The PBG presented higher affinity to polydatin (Km = 0.74 mmol L−1) than p‐nitrophenyl‐β‐d‐glucopyranoside (Km = 2.9 mmol L−1) and cellobiose (Km = 8.9 mmol L−1).
CONCLUSION
With this enzyme, nearly all polydatin in P. cuspidatum was converted to resveratrol. Although several β‐D‐glucosidases (BGLs) have been obtained from other sources, PBG is distinguished from other BGLs by its outstanding thermal stability and high catalytic efficiency. © 2015 Society of Chemical Industry BACKGROUND Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum . Resveratrol has become the subject of intensive research over the past two decades owing to its outstanding pharmacological properties. However, its lower concentration in plants compared to polydatin limits its application. In this study, the polydatin- beta -d-glucosidase (PBG) that hydrolyzes the beta -d-glucosyl residue of polydatin with release of resveratrol was purified to homogeneity and characterized. RESULTS The molecular weight of PBG was estimated to be 125 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 128 kDa by size-exclusion chromatography- multi-angle laser light scattering/ultraviolet/refractive index. The optimal PBG activity was observed at 70 degree C and pH 4.5. The enzyme showed around 50% stability at 60 degree C for 12h and residual activity was over 80% at pH 3.0-5.0. Ca super(2+), Mg super(2+), Mn super(2+), Zn super(2+), Ba super(2+), Ni super(2+), Co super(2+) and Cu super(2+) ions had no significant effect on the enzyme activity. The PBG presented higher affinity to polydatin ( K sub(m)=0.74mmolL super(-1)) than p -nitrophenyl- beta -d-glucopyranoside ( K sub(m)=2.9mmolL super(-1)) and cellobiose ( K sub(m)=8.9mmolL super(-1)). CONCLUSION With this enzyme, nearly all polydatin in P. cuspidatum was converted to resveratrol. Although several beta -D-glucosidases (BGLs) have been obtained from other sources, PBG is distinguished from other BGLs by its outstanding thermal stability and high catalytic efficiency. Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum. Resveratrol has become the subject of intensive research over the past two decades owing to its outstanding pharmacological properties. However, its lower concentration in plants compared to polydatin limits its application. In this study, the polydatin-β-d-glucosidase (PBG) that hydrolyzes the β-d-glucosyl residue of polydatin with release of resveratrol was purified to homogeneity and characterized. The molecular weight of PBG was estimated to be 125 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and 128 kDa by size-exclusion chromatography- multi-angle laser light scattering/ultraviolet/refractive index. The optimal PBG activity was observed at 70 °C and pH 4.5. The enzyme showed around 50% stability at 60 °C for 12 h and residual activity was over 80% at pH 3.0-5.0. Ca(2+) , Mg(2+) , Mn(2+) , Zn(2+) , Ba(2+) , Ni(2+) , Co(2+) and Cu(2+) ions had no significant effect on the enzyme activity. The PBG presented higher affinity to polydatin (Km = 0.74 mmol L(-1) ) than p-nitrophenyl-β-d-glucopyranoside (Km = 2.9 mmol L(-1) ) and cellobiose (Km = 8.9 mmol L(-1) ). With this enzyme, nearly all polydatin in P. cuspidatum was converted to resveratrol. Although several β-D-glucosidases (BGLs) have been obtained from other sources, PBG is distinguished from other BGLs by its outstanding thermal stability and high catalytic efficiency. © 2015 Society of Chemical Industry. BACKGROUND: Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum. Resveratrol has become the subject of intensive research over the past two decades owing to its outstanding pharmacological properties. However, its lower concentration in plants compared to polydatin limits its application. In this study, the polydatin‐β‐d‐glucosidase (PBG) that hydrolyzes the β‐d‐glucosyl residue of polydatin with release of resveratrol was purified to homogeneity and characterized. RESULTS: The molecular weight of PBG was estimated to be 125 kDa by sodium dodecyl sulfate–polyacrylamide gel electrophoresis and 128 kDa by size‐exclusion chromatography– multi‐angle laser light scattering/ultraviolet/refractive index. The optimal PBG activity was observed at 70 °C and pH 4.5. The enzyme showed around 50% stability at 60 °C for 12 h and residual activity was over 80% at pH 3.0–5.0. Ca²⁺, Mg²⁺, Mn²⁺, Zn²⁺, Ba²⁺, Ni²⁺, Co²⁺ and Cu²⁺ ions had no significant effect on the enzyme activity. The PBG presented higher affinity to polydatin (Kₘ = 0.74 mmol L⁻¹) than p‐nitrophenyl‐β‐d‐glucopyranoside (Kₘ = 2.9 mmol L⁻¹) and cellobiose (Kₘ = 8.9 mmol L⁻¹). CONCLUSION: With this enzyme, nearly all polydatin in P. cuspidatum was converted to resveratrol. Although several β‐D‐glucosidases (BGLs) have been obtained from other sources, PBG is distinguished from other BGLs by its outstanding thermal stability and high catalytic efficiency. © 2015 Society of Chemical Industry |
| Author | Jiang, Bo Mu, Wanmeng Li, Shuhua Zhou, Linfang Zhang, Tao |
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| Keywords | Aspergillus niger SK34.002 polydatin-β-d-glucosidase characterization resveratrol purification |
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| References_xml | – reference: Pitson SM, Seviour RJ and McDougall BM, Purification and characterization of an extracellular beta-glucosidase from the filamentous fungus Acremonium persicinum and its probable role in beta-glucan degradation. Enzyme Microb Technol 21:182-190 (1997). – reference: Joo A-R, Jeya M, Lee K-M, Lee K-M, Moon H-J, Kim Y-S et al., Production and characterization of β-1,4-glucosidase from a strain of Penicillium pinophilum. Process Biochem 45:851-858 (2010). – reference: Bhiri F, Chaabouni SE, Limam F, Ghrir R and Marzouki N, Purification and biochemical characterization of extracellular beta-glucosidases from the hypercellulolytic Pol6 mutant of Penicillium occitanis. Appl Biochem Biotechnol 149:169-182 (2008). – reference: Valaskova V and Baldrian P, Degradation of cellulose and hemicelluloses by the brown rot fungus Piptoporus betulinus: production of extracellular enzymes and characterization of the major cellulases. 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Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum. Resveratrol has become the subject of intensive research... Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum. Resveratrol has become the subject of intensive research over the past... BACKGROUND Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum . Resveratrol has become the subject of intensive research... BACKGROUND: Resveratrol and its glucoside polydatin are the main stilbenes in Polygonum cuspidatum. Resveratrol has become the subject of intensive research... |
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| SubjectTerms | Amino Acid Sequence Aspergillus niger Aspergillus niger - enzymology Aspergillus niger - metabolism Aspergillus niger SK34.002 barium beta-glucosidase beta-Glucosidase - antagonists & inhibitors beta-Glucosidase - metabolism Biotechnology - methods Biotransformation calcium Catalysts catalytic activity cellobiose characterization cobalt copper Electrophoresis enzyme activity Enzymes Gene Expression Regulation, Enzymologic Gene Expression Regulation, Fungal glucosides Glucosides - metabolism Homogeneity ions Light scattering magnesium manganese medicinal properties Metals Molecular Sequence Data molecular weight nickel polyacrylamide gel electrophoresis polydatin-β-d-glucosidase Polygonum cuspidatum purification refractive index resveratrol Reynoutria japonica Sodium Stilbenes - chemistry Stilbenes - metabolism Substrate Specificity thermal stability Ultraviolet zinc |
| Title | Properties of a novel polydatin-β-d-glucosidase from Aspergillus niger SK34.002 and its application in enzymatic preparation of resveratrol |
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