Characterization and Application of BiLA, a Psychrophilic α‑Amylase from Bifidobacterium longum

In this study, a novel α-amylase was cloned from Bifidobacterium longum and named BiLA. The enzyme exhibited optimal activity at 20 °C and a pH value of 5.0. Kinetic analysis using various carbohydrate substrates revealed that BiLA had the highest k cat/K m value for amylose. Interestingly, analysis...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2016-04, Vol.64 (13), p.2709-2718
Main Authors: Lee, Hye-Won, Jeon, Hye-Yeon, Choi, Hye-Jeong, Kim, Na-Ri, Choung, Woo-Jae, Koo, Ye-Seul, Ko, Dam-Seul, You, SangGuan, Shim, Jae-Hoon
Format: Article
Language:English
Subjects:
alpha-Amylases - genetics
alpha-Amylases - metabolism
Amylose - analysis
Amylose - metabolism
Animals
Bifidobacterium - enzymology
Electrophoresis, Polyacrylamide Gel
Glucan 1,4-alpha-Glucosidase - metabolism
Hydrolysis
Kinetics
Pancreatic alpha-Amylases - metabolism
Starch - chemistry
Swine
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Summary:In this study, a novel α-amylase was cloned from Bifidobacterium longum and named BiLA. The enzyme exhibited optimal activity at 20 °C and a pH value of 5.0. Kinetic analysis using various carbohydrate substrates revealed that BiLA had the highest k cat/K m value for amylose. Interestingly, analysis of the enzymatic reaction products demonstrated that BiLA specifically catalyzed the hydrolysis of oligosaccharides and starches up to G5 from the nonreducing ends. To determine whether BiLA can be used to generate slowly digestible starch (SDS), starch was treated with BiLA, and the kinetic parameters were analyzed using porcine pancreatic α-amylase (PPA) and amyloglucosidase (AMG). Compared to normal starch, BiLA-treated starch showed lower k cat/K m values with PPA and AMG, suggesting that BiLA is a potential candidate for the production of SDS.
ISSN:0021-8561
1520-5118
DOI:10.1021/acs.jafc.5b05904