| Title | Functional expression and enzymatic characterization of Lactobacillus plantarum cyclomaltodextrinase catalyzing novel acarbose hydrolysis |
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| Author | Myoung-Uoon Jang1, Hye-Jeong Kang2, Chang-Ku Jeong3, Yewon Kang1, Ji-Eun Park1, and Tae-Jip Kim1* |
| Address | 1Division of Animal, Horticultural and Food Sciences, Graduate School of Chungbuk National University, Cheongju 28644, Republic of Korea, 2Chungcheongbuk-do Agricultural Research and Extension Services, Cheongju 28130, Republic of Korea, 3Advanced Protein Technologies Co., Suwon 16229, Republic of Korea |
| Bibliography | Journal of Microbiology, 56(2),113–118, 2018, |
| DOI | 10.1007/s12275-018-7551-3 |
| Key Words | Lactobacillus plantarum, cyclomaltodextrinase, functional expression, novel acarbose hydrolysis, acarviosine |
| Abstract | Cyclomaltodextrinases (CDases) belong to Glycoside Hydrolases (GH) family 13, which show versatile hydrolyzing and/or transglycosylation activity against cyclodextrin (CD), starch, and pullulan. Especially, some CDases have been reported to hydrolyze acarbose, a potent α-glucosidase inhibitor, and transfer the resulting acarviosine-glucose to various acceptors. In this study, a novel CDase (LPCD) gene was cloned from Lactobacillus plantarum WCFS1, which encodes 574 amino acids (64.6 kDa) and shares less than 44% of identities with the known CDase-family enzymes. Recombinant LPCD with C-terminal six-histidines was produced and purified from Escherichia coli. It showed the highest activity on β-CD at 45°C and pH 5.0, respectively. Gel permeation chromatography analysis revealed that LPCD exists as a dodecameric form (~826 kDa). Its hydrolyzing activity on β- CD is almost same as that on starch, whereas it can hardly attack pullulan. Most interestingly, LPCD catalyzed the unique modes of action in acarbose hydrolysis to produce maltose and acarviosine, as well as to glucose and acarviosineglucose. |