A Novel Maltogenic Amylase CoMA from Corallococcus sp. EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose.

A Novel Maltogenic Amylase CoMA from Corallococcus sp. EGB Catalyzes the Conversion of Maltooligosaccharides and Soluble Starch to Maltose. Appl Environ Microbiol. 2018 May 11;: Authors: Zhou J, Li Z, Zhang H, Wu J, Ye X, Dong W, Jiang M, Huang Y, Cui Z Abstract Here, a novel amylolytic enzyme gene designated coMA was cloned from Corallococcus sp. EGB. The deduced amino acid sequence contained a predicted lipoprotein signal peptide (residues 1-18) and conserved glycoside hydrolase family 13 (GH13) module. The amino acid sequence of CoMA exhibits low sequence identity (10-19%) with cyclodextrin-hydrolyzing enzymes (GH13_20) and is assigned to GH13_36. The most outstanding feature of CoMA is its ability to catalyze the conversion of maltooligosaccharides (≥ G3) and soluble starch to maltose as the sole hydrolysate. Moreover, it can hydrolyze γ-cyclodextrin and starch to maltose and hydrolyze pullulan exclusively to panose with relative activities of 0.2, 1 and 0.14, respectively. CoMA showed both hydrolysis and transglycosylation activities toward α-1,4-glycosidic bonds but not to α-1,6-linkages. And glucosyl-transfer was postulated to be the major transglycosidation reaction for producing a high level of maltose without the attendant production of glucose. These results indicated that CoMA possesses some unusual properties that distinguishes it from maltogenic amylases and typical α-amylases. Its physicochemical properties sugge...
Source: Applied and Environmental Microbiology - Category: Microbiology Authors: Tags: Appl Environ Microbiol Source Type: research