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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27139

Title: Protein Engineering of Sulfolobus solfataricus Maltooligosyltrehalose Synthase To Alter Its Selectivity
Authors: Tsuei-Yun Fang;Wen-Chi Tseng;Ching-Hsing Pan;Yao-Te Chun;Mei-Ying Wang
Contributors: NTOU:Department of Food Science
國立臺灣海洋大學:食品科學系
Keywords: Maltooligosyltrehalose synthase;selectivity;site-directed mutagenesis;trehalose;substrate specificity;Sulfolobus
Date: 2007-07
Issue Date: 2011-10-21T02:23:42Z
Publisher: Journal of Agricultural and Food Chemistry
Abstract: Abstract:Maltooligosyltrehalose synthase (MTSase) is one of the key enzymes involved in trehalose production from starch and catalyzes an intramolecular transglycosylation reaction by converting the α-1,4- to α,α-1,1-glucosidic linkage. Mutations at residues F206, F207, and F405 were constructed to change the selectivity of the enzyme because the changes in selectivity could reduce the side hydrolysis reaction of releasing glucose and thus increase trehalose production from starch. As compared with wild-type MTSase, F405Y and F405M MTSases had decreased ratios of the initial rate of glucose formation to that of trehalose formation in starch digestion at 75 °C when wild-type and mutant MTSases were, respectively, used with isoamylase and maltooligosyltrehalose trehalohydrolase (MTHase). The highest trehalose yield from starch digestion was by the mutant MTSase having the lowest initial rate of glucose formation to trehalose formation, and this predicted high trehalose yield better than the ratio of catalytic efficiency for hydrolysis to that for transglycosylation.
Relation: 55(14), pp.5588–5594
URI: http://ntour.ntou.edu.tw/handle/987654321/27139
Appears in Collections:[食品科學系] 期刊論文

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