Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
17697 | Enzyme and Microbial Technology | 2010 | 7 Pages |
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.