کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
17697 | 42690 | 2010 | 7 صفحه PDF | دانلود رایگان |
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.
Journal: Enzyme and Microbial Technology - Volume 46, Issue 5, 5 April 2010, Pages 331–337