http://scholars.ntou.edu.tw/handle/123456789/8593
DC 欄位 | 值 | 語言 |
---|---|---|
dc.contributor.author | Fang, TY | en_US |
dc.contributor.author | Hung, XG | en_US |
dc.contributor.author | Shih, TY | en_US |
dc.contributor.author | Tseng, WC | en_US |
dc.date.accessioned | 2020-11-20T11:17:32Z | - |
dc.date.available | 2020-11-20T11:17:32Z | - |
dc.date.issued | 2004-08 | - |
dc.identifier.issn | 1431-0651 | - |
dc.identifier.uri | http://scholars.ntou.edu.tw/handle/123456789/8593 | - |
dc.description.abstract | The trehalosyl dextrin-forming enzyme (TDFE) mainly catalyzes an intramolecular transglycosyl reaction to form trehalosyl dextrins from dextrins by converting the alpha-1,4-glucosidic linkage at the reducing end to an alpha-1,1-glucosidic linkage. In this study, the treY gene encoding TDFE was PCR cloned from the genomic DNA of Sulfolobus solfataricus ATCC 35092 to an expression vector with a T7 lac promoter and then expressed in Escherichia coli. The recombinant TDFE was purified sequentially by using heat treatment, ultrafiltration, and gel filtration. The obtained recombinant TDFE showed an apparent optimal pH of 5 and an optimal temperature of 75degreesC. The enzyme was stable in a pH range of 4.5-11, and the activity remained unchanged after a 2-h incubation at 80degreesC. The transglycosylation activity of TDFE was higher when using maltoheptaose as substrate than maltooligosaccharides with a low degree of polymerization (DP). However, the hydrolysis activity of TDFE became stronger when low DP maltooligosaccharides, such as maltotriose, were used as substrate. The ratios of hydrolysis activity to transglycosylation activity were in the range of 0.2-14% and increased when the DP of substrate decreased. The recombinant TDFE was found to exhibit different substrate specificity, such as its preferred substrates for the transglycosylation reaction and the ratio of hydrolysis to transglycosylation of the enzyme reacting with maltotriose, when compared with other natural or recombinant TDFEs from Sulfolobus. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | SPRINGER JAPAN KK | en_US |
dc.relation.ispartof | Extremophiles | en_US |
dc.subject | Escherichia coli | en_US |
dc.subject | starch | en_US |
dc.subject | Sulfolobus trehalose | en_US |
dc.subject | trehalosyl dextrin-forming enzyme | en_US |
dc.subject | AWAMORI GLUCOAMYLASE SELECTIVITY | en_US |
dc.subject | HYPERTHERMOPHILIC ARCHAEUM | en_US |
dc.subject | SACCHAROMYCES-CEREVISIAE | en_US |
dc.subject | KM1 | en_US |
dc.subject | ACIDOCALDARIUS | en_US |
dc.subject | STARCH | en_US |
dc.subject | PURIFICATION | en_US |
dc.subject | TOLERANCE | en_US |
dc.subject | MECHANISM | en_US |
dc.subject | MUTATIONS | en_US |
dc.title | Characterization of the trehalosyl dextrin-forming enzyme from the thermophilic archaeon Sulfolobus solfataricus ATCC 35092 | en_US |
dc.type | journal article | en_US |
dc.identifier.doi | 10.1007/s00792-004-0393-4 | - |
dc.identifier.isi | WOS:000223264300009 | - |
dc.relation.journalvolume | 8 | en_US |
dc.relation.journalissue | 4 | en_US |
dc.relation.pages | 335-343 | en_US |
item.cerifentitytype | Publications | - |
item.languageiso639-1 | en_US | - |
item.fulltext | no fulltext | - |
item.openairetype | journal article | - |
item.grantfulltext | none | - |
item.openairecristype | http://purl.org/coar/resource_type/c_6501 | - |
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。