Kinetics and Mechanism of Hydrolysis of Phenyl α-Maltoside by Saccharifying α-Amylase of Bacillus subtilis*

Yoshida, Hozumi; Kitano, Hiromi; Ono, Satoshi

doi:10.1093/oxfordjournals.jbchem.a129072

Cited by 17 publications

(4 citation statements)

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“…. However, no maltotriose was detected at the concentration of 17.5 mmol/L of glucose and 5.3 mmol/L maltose in the presence of AmyC (data not shown), suggesting the formation of maltotetraose cannot be attributed to the secondary synthetic reaction . Maltotriose and maltotetraose were observed during maltose cleavage by saccharifying amylase from Bacillus subtilis by glycosyl transfer .…”

Section: Resultsmentioning

confidence: 94%

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

Xia

et al. 2015

Starch Stärke

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A novel amylase AmyC gene (amyC) from Corallococcus sp. EGB was cloned and expressed in Esherichia coli. Analysis of the sequence homology showed that AmyC shared 92% identity with the putative a-amylase from Corallococcus coralloides DSM 2259 and formed a separate branch from other amylases. The recombinant AmyC (rAmyC) was purified and biochemically characterized. rAmyC hydrolyzes various starch and maltooligosaccharides larger than G4 to glucose to maltotetraose without production of other oligosaccharides, indicating that it is a special saccharifying a-amylase. AmyC possesses weak but significant a-1, 6-bond cleaving activity and transglycosylation activity. The time course of the reaction with maltotriose as a substrate evidently showed the formation of oligosaccharide of degree of polymerization (DP4) by glycosyl transfer. The substrate specificities and end products analysis showed that the hydrolytic pattern of rAmyC is unique. rAmyC exhibited maximum hydrolysis activity at 50°C in 50 mM sodium phosphate buffer (pH 6.0) with a specific activity of 180 U/mg. Its activity towards starch was independent of calcium ions and activated by dithiothreitol. These results indicate that AmyC is a novel endo multifunctional amylase possessing distinct characteristics.

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Section: Resultsmentioning

confidence: 94%

“…We suspect that maltotriose is not cleaved by hydrolysis. Transglycosylation or condensation may involve the formation of maltotetraose catalyzed by AmyC .…”

Section: Resultsmentioning

confidence: 99%

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

Xia

et al. 2015

Starch Stärke

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“…7, together with the chromatograms relating to the reaction products to which p-maltose (B) or the equilibrium mixture of a-and pmaltose (C) is added. It was confirmed that aG, aG 2 , the substituted phenyl (pN¢, pTB¢, pE¢ or pCI¢) a-glucoside, maltotriose (G 3 ) as a side reaction product 12 ) and a trace amount of pG, which also appeared to occur through spontaneous mutarotation, were produced from each substrate. The relative values of the retention time for the TMS-derivatives of these products are listed in Table III.…”

Section: Anomeric Forms Of the Products From Substituted Phenyl A-malmentioning

confidence: 87%

Quantitative Study of Anomeric Forms of Maltose Produced by α- andβAmylases

Kimura¹,

Chiba²

1983

Agricultural and Biological Chemistry

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“…Ki" [ESS] [I] (12) [ESSI] A: The slopes of the primary plots in Fig. 4 were replotted against the inhibitor concentration.…”

Section: Inhibition Studiesmentioning

confidence: 99%

Kinetic Properties of Galactose Oxidase fromGibberella fujikuroi

Aisaka¹,

Uwajima²,

Terada³

1984

Agricultural and Biological Chemistry

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Kinetics and Mechanism of Hydrolysis of Phenyl α-Maltoside by Saccharifying α-Amylase of Bacillus subtilis*

Cited by 17 publications

References 0 publications

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

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

Quantitative Study of Anomeric Forms of Maltose Produced by α- andβAmylases

Kinetic Properties of Galactose Oxidase fromGibberella fujikuroi

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