http://scholars.ntou.edu.tw/handle/123456789/22126
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Wen-Chi Tseng | en_US |
dc.contributor.author | Yu-Chun Chen | en_US |
dc.contributor.author | Hao-Chin Chang | en_US |
dc.contributor.author | Chia-Jui Lin | en_US |
dc.contributor.author | Tsuei-Yun Fang | en_US |
dc.date.accessioned | 2022-09-12T03:17:16Z | - |
dc.date.available | 2022-09-12T03:17:16Z | - |
dc.date.issued | 2022-08-27 | - |
dc.identifier.uri | http://scholars.ntou.edu.tw/handle/123456789/22126 | - |
dc.description.abstract | L-Rhamnose isomerase (L-RhI) catalyzes rare sugar isomerization between aldoses and ketoses. In an attempt to alter the substrate specificity of Thermoanaerobacterium saccharolyticus NTOU1 L-RhI (TsRhI), residue Ile102 was changed to other polar or charged amino acid residues by site-directed mutagenesis. The results of activity-screening using different substrates indicate that I102N, I102Q, and I102R TsRhIs can increase the preference against D-allose in comparison with the wild-type enzyme. The catalytic efficiencies of the purified I102N, I102Q, and I102R TsRhIs against D-allose are 148 %, 277 %, and 191 %, respectively, of that of wild-type enzyme, while those against L-rhamnose are 100 %, 167 % and 87 %, respectively. Mutant I102N, I102Q, and I102R TsRhIs were noted to have the altered substrate specificity, and I102Q TsRhI has the highest catalytic efficiency against D-allose presumably through the formation of an additional hydrogen bond with D-allose. The purified wild-type and mutant TsRhIs were further used to produce D-allose from 100 g/L D-fructose in the presence of D-allulose 3-epimerase, and the yields can reach as high as 22 % D-allulose and 12 % D-allose upon equilibrium. I102Q TsRhI takes only around half of the time to reach the same 12 % D-allose yield, suggesting that this mutant enzyme has a potential to be applied in D-allose production. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | Elsevier | en_US |
dc.relation.ispartof | Journal of Biotechnology | en_US |
dc.subject | L-rhamnose isomerase | en_US |
dc.subject | D-allose | en_US |
dc.subject | D-allulose | en_US |
dc.subject | Thermoanaerobacterium saccharolyticum | en_US |
dc.subject | mutagenesis | en_US |
dc.title | Altering the substrate specificity of recombinant L-rhamnose isomerase from Thermoanaerobacterium saccharolyticum NTOU1 to favor D-allose production | en_US |
dc.type | journal article | en_US |
dc.identifier.doi | 10.1016/j.jbiotec.2022.08.015 | - |
dc.relation.journalvolume | 358 | en_US |
dc.relation.pages | 9-16 | en_US |
item.fulltext | no fulltext | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
item.grantfulltext | none | - |
item.languageiso639-1 | en_US | - |
item.openairetype | journal article | - |
crisitem.author.dept | College of Life Sciences | - |
crisitem.author.dept | Department of Food Science | - |
crisitem.author.dept | National Taiwan Ocean University,NTOU | - |
crisitem.author.parentorg | National Taiwan Ocean University,NTOU | - |
crisitem.author.parentorg | College of Life Sciences | - |
顯示於: | 食品科學系 |
在 IR 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。