The effects of multiple mutations of substrate-binding subsite residues on the activity and substrate selectivity of maltooligosyltrehalose trehalohydrolase from Sulfolobus solfataricus ATCC 35092
碩士 === 國立臺灣海洋大學 === 食品科學系 === 96 === Maltooligosyltrehalose trehalohydrolase (MTHase) mainly hydrolyzes the α-1, 4 linkage adjacent to the α-1, 1 bond of maltooligosyltrehalose to release trehalose, and it can also hydrolyze the α-1, 4 linkage at the reducing end of maltooligosaccharides to release...
| Main Authors: | , |
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| Other Authors: | |
| Format: | Others |
| Language: | zh-TW |
| Published: |
2008
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| Online Access: | http://ndltd.ncl.edu.tw/handle/29685951308559977976 |