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Transglycosylation reactions of Thermotoga maritima α-amylase

Paper ID Volume ID Publish Year Pages File Format Full-Text
17697 42690 2010 7 PDF Available
Title
Transglycosylation reactions of Thermotoga maritima α-amylase
Abstract

The capacity of Amy A, a α-amylase from the hyperthermophilic bacteria Thermotoga maritima to carry out transfer reactions in addition to hydrolysis was investigated. Amy A is a saccharifying enzyme that catalyzes the hydrolysis of internal α-1,4 linkages of glucose polymers generating low molecular weight products (G1–G7); however, in the long term it is capable of producing glucose and maltose exclusively. It was shown that Amy A is able to transform maltose to higher molecular weight oligosaccharides like maltoheptaose, through a combination of transfer and hydrolysis reactions: the fact that the enzyme can use maltose to generate higher molecular weight products is an almost unique property among α-amylases, with neotrehalose as one of the products of the transglucosylation activity. Amy A is also capable of efficiently performing alcoholysis reactions from starch and maltodextrins to methanol and butanol, generating alkyl-glycosides. This is the first report in the scientific literature concerning the synthesis of neotrehalose by an α-amylase.

Keywords
α-Amylase; Thermotoga maritima; Transglycosylation; Alcoholysis; Alkyl-glycosides; Neotrehalose
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Transglycosylation reactions of Thermotoga maritima α-amylase
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 46, Issue 5, 5 April 2010, Pages 331–337
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us