Abstract:
:Debranching of (1, 6)-α-linkages in starch is of great significance as it is widely used in different industries. In recent years, identifying a single potential enzyme that could debranch (1, 6)-α-linkages and cleave (1, 4)-α-linkages brought great interest as amylopectin possessed both (1, 4)-α- and (1, 6)-α-linkages. In the present study, a 64\,kDa exo-α-l, 4-glucosidase from Bacillus pseudofirmus 703, annotated as Amy112, was cloned and characterized. Biochemical analysis indicated that heterologous Amy112 expressed in Escherichia coli exhibited a high activity against amylopectin, with the optimal temperature and pH of 40°C and pH 7.0, respectively. Addition of K+ ions improved the amy112 activity by 12%, but Li+, Ca2+ and Mg2+ ions showed no significant effect. Amy112 sequence homology revealed that it belonged to glycoside hydrolase family 13, showing 65% identity with α-glucosidase GSJ from Geobacillus sp. HTA-462. This is the first report indicating that Amy112 from B. pseudofirmus 703 belongs to GH13 enzyme family, having both exo-α-1, 4-glucosidase and oligo-l, 6-glucosidase activities. However, no transglycosylation activity was detected in LC-MS analysis. Amy112 would be of great significance of being utilized to debranch starch in different industries in a cost effective manner.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Wang S,Wang Q,Zhou Y,Lu Z,Zhang G,Ma Ydoi
10.1016/j.ijbiomac.2017.03.129subject
Has Abstractpub_date
2017-08-01 00:00:00pages
973-982eissn
0141-8130issn
1879-0003pii
S0141-8130(17)30338-0journal_volume
101pub_type
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