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http://dx.doi.org/10.4014/mbl.1608.08008

Gene Cluster Analysis and Functional Characterization of Cyclomaltodextrinase from Listeria innocua  

Jang, Myoung-Uoon (Division of Animal, Horticultural, and Food Sciences, Graduate School of Chungbuk National University)
Jeong, Chang-Ku (Advanced Protein echnologies Co.)
Kang, Hye-Jeong (Division of Animal, Horticultural, and Food Sciences, Graduate School of Chungbuk National University)
Kim, Min-Jeong (Division of Animal, Horticultural, and Food Sciences, Graduate School of Chungbuk National University)
Lee, Min-Jae (Division of Animal, Horticultural, and Food Sciences, Graduate School of Chungbuk National University)
Son, Byung Sam (Division of Animal, Horticultural, and Food Sciences, Graduate School of Chungbuk National University)
Kim, Tae-Jip (Division of Animal, Horticultural, and Food Sciences, Graduate School of Chungbuk National University)
Publication Information
Microbiology and Biotechnology Letters / v.44, no.3, 2016 , pp. 363-369 More about this Journal
Abstract
A putative cyclomaltodextrinase gene (licd) was found from the genome of Listeria innocua ATCC 33090. The licd gene is located in the gene cluster involved in maltose/maltodextrin utilization, which consists of various genes encoding maltose phosphorylase and sugar ABC transporters. The structural gene encodes 591 amino acids with a predicted molecular mass of 68.6 kDa, which shares less than 58% of amino acid sequence identity with other known CDase family enzymes. The licd gene was cloned, and the dimeric enzyme with C-terminal six-histidines was successfully produced and purified from recombinant Escherichia coli. The enzyme showed the highest activity at pH 7.0 and 37℃. licd could hydrolyze β-cyclodextrin, starch, and maltotriose to mainly maltose, and it cleaved pullulan to panose. It could also catalyze the hydrolysis of acarbose to glucose and acarviosine-glucose. In particular, it showed significantly higher activity towards β-cyclodextrin and maltotriose than towards starch and acarbose. licd also showed transglycosylation activity, producing α-(1,6)- and/or α-(1,3)-linked transfer products from the acarbose donor and α-methyl glucopyranoside acceptor.
Keywords
Listeria innocua; cyclomaltodextrinase (CDase); gene cluster; enzymatic characterization;
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