Molecular cloning and characterization of a novel GH13 saccharifying α‐amylase AmyC from <i>Corallococcus</i> sp. EGB

Wu, Jiale; Xia, Bingjie; Li, Zhoukun; Ye, Xianfeng; Chen, Qiongzhen; Dong, Weiliang; Zhou, Jie; Huang, Yan; Cui, Zhongli

doi:10.1002/star.201400258

Cited by 5 publications

(4 citation statements)

References 43 publications

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“…strain EGB. We isolated and characterized a novel liquefying maltohexaose-forming ␣-amylase (AmyM) and saccharifying ␣-amylase (AmyC) from the EGB strain (26,27). We assumed that AmyM is the main extracellular liquefying amylase for utilizing starch in Corallococcus sp.…”

Section: Resultsmentioning

confidence: 99%

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

Zhou

Zhang

et al. 2018

Appl Environ Microbiol

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The gene encoding the novel amylolytic enzyme designated CoMA was cloned from sp. strain EGB. The deduced amino acid sequence contained a predicted lipoprotein signal peptide (residues 1 to 18) and a conserved glycoside hydrolase family 13 (GH13) module. The amino acid sequence of CoMA exhibits low sequence identity (10 to 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. Moreover, 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 distinguish it from maltogenic amylases and typical α-amylases. Its physicochemical properties suggested that it has potential for commercial development. The α-amylase from sp. EGB, which was classified to the GH13_36 subfamily, can catalyze the conversion of maltooligosaccharides (≥G3) and soluble starch to maltose as the sole hydrolysate. An action mechanism for producing a high level of maltose without the attendant production of glucose has been proposed. Moreover, it also can hydrolyze γ-cyclodextrin and pullulan. Its biochemical characterization suggested that CoMA may be involved the accumulation of maltose in media.

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Section: Resultsmentioning

confidence: 99%

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

Zhou

Zhang

et al. 2018

Appl Environ Microbiol

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“…Bacteriolytic myxobacteria can utilize several polysaccharides and maltotriose as carbon source, but mono-or disaccharides do not stimulate growth [45]. Several new glycoside hydrolases from Corallococcus species, including some from family GH13, have already been characterised in the past few years [46][47][48][49][50][51]. Those GH13 hydrolases indeed process maltooligosaccharides, but the GH13 phosphorylase discussed in this work did not appear to show such activity.…”

Section: Discussionmentioning

confidence: 68%

A GH13 glycoside phosphorylase with unknown substrate specificity from Corallococcus coralloides

Franceus

Desmet

2019

Amylase

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Glycoside phosphorylases in subfamily GH13_18 of the carbohydrate-active enzyme database CAZy catalyse the reversible phosphorolysis of α-glycosidic bonds. They contribute to a more energy-efficient metabolism in vivo, and can be applied for the synthesis of valuable glucosides, sugars or sugar phosphates in vitro. Continuing our efforts to uncover new phosphorylase specificities, we identified an enzyme from the myxobacterium Corallococcus coralloides DSM 2259 that does not feature the signature sequence patterns of previously characterised phosphorylases. The enzyme was recombinantly expressed and subjected to substrate screening. Although it was confirmed that the Corallococcus phosphorylase does not have the same substrate specificity as other phoshorylases from subfamily GH13_18, its true natural substrate remains a mystery for now. Myxobacteria have been widely investigated as producers of numerous bioactive secondary metabolites for decades, but little research has been conducted on myxobacterial proteins. The present study exemplifies the untapped metabolic activities and functional diversity that these fascinating organisms may have left to show.

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Section: Substrate Speci City Of Amyflamentioning

confidence: 99%

“…Except that, Wu et al (2015) reported the amylase AmyC from Corallococcus sp. EGB showed the highest hydrolytic activity on potato starch, and its activity was 21% higher than that on soluble starch (23). Similar results were found in the α-amylase RoAmy of Rhizopus oryzae, RoAmy exhibited the highest activity on wheat starch and corn starch, which was about 30% higher than that on soluble starch (24).…”

Section: Substrate Speci City Of Amyflamentioning

confidence: 99%

Heterologous Expression and Characterization of a Novel Mesophilic Maltogenic α-Amylase AmyFlA from Flavobacterium sp. NAU1659

Wang,

Xie,

Yan

et al. 2024

Appl Biochem Biotechnol

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A novel amylase AmyFlA from Flavobacterium sp. NAU1659 was cloned and expressed in Esherichia coli. Analysis of the sequence homology exhibited that AmyFlA shared 98% identity with the putative protein belonging to glycoside hydrolase family 13 (GH13) from Flavobacterium sp., however, it had the sequence identity lower than 35% with the reported GH13 amylases. AmyFlA was consisted of 620 amino acids, with a putative signal peptide of 25 amino acids. The enzyme enabled to hydrolyze soluble starch into a high level of maltose, and showed a speci c activity of 352.97 U/mg at 50°C in 50 mM phosphate buffer (pH 6.0). The K m and V max of AmyFlA was 3.15 mg/ml and 566.36 µmol•ml − 1 •min − 1 under optimal condition, respectively. Moreover, compared to the reported maltogenic amylases, at the initial reaction, AmyFlA produced a less variety of intermediate oligosaccharides, in which contained a higher amount of maltose. These results indicated that AmyFlA possessed potential application values in high-maltose syrup production.

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Molecular cloning and characterization of a novel GH13 saccharifying α‐amylase AmyC from Corallococcus sp. EGB

Cited by 5 publications

References 43 publications

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

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

A GH13 glycoside phosphorylase with unknown substrate specificity from Corallococcus coralloides

Heterologous Expression and Characterization of a Novel Mesophilic Maltogenic α-Amylase AmyFlA from Flavobacterium sp. NAU1659

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