Please use this identifier to cite or link to this item: http://hdl.handle.net/11455/68892
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dc.contributor.authorChang, C.T.en_US
dc.contributor.authorLo, H.F.en_US
dc.contributor.authorChi, M.C.en_US
dc.contributor.authorYao, C.Y.en_US
dc.contributor.authorHsu, W.H.en_US
dc.contributor.authorLin, L.L.en_US
dc.date2003zh_TW
dc.date.accessioned2014-06-11T05:57:28Z-
dc.date.available2014-06-11T05:57:28Z-
dc.identifier.issn1431-0651zh_TW
dc.identifier.urihttp://hdl.handle.net/11455/68892-
dc.description.abstractTo understand the structure-function relationships of a truncated Bacillus sp. strain TS-23 alpha-amylase, each of His-137, His-191, His-239, His-269, His-305, His-323, His-361, His-436, and His-475 was replaced with leucine. The molecular masses of the purified wild-type and mutant enzymes were approximately 54 kDa. The specific activity of His323Leu and His436Leu was decreased by more than 52%, while His239Leu, His305Leu, and His475Leu showed activity similar to that of the wild-type enzyme. As compared with the wild-type enzyme, His323Leu and His436Leu exhibited a 62% decrease in the value of k(cat)/K-m. Alterations in His-191, His-239, His-305, and His-475 did not cause a significant change in the K-m or k(cat) values. At 70degreesC, a decreased half-life was observed in His436Leu. These results indicate that His-137, His-269, and His-361 of Bacillus sp. strain TS-23 alpha-amylase are important for proper catalytic activity and that His-436 may contribute to the thermostability of the enzyme.en_US
dc.language.isoen_USzh_TW
dc.relationExtremophilesen_US
dc.relation.ispartofseriesExtremophiles, Volume 7, Issue 6, Page(s) 505-509.en_US
dc.relation.urihttp://dx.doi.org/10.1007/s00792-003-0341-8en_US
dc.subjectalpha-amylaseen_US
dc.subjectBacillus sp TS-23en_US
dc.subjecthistidineen_US
dc.subjectsite-directed mutagenesisen_US
dc.subjectamino-acid-sequenceen_US
dc.subjectnucleotide-sequenceen_US
dc.subjectcyclodextrinen_US
dc.subjectglycosyltransferaseen_US
dc.subjectbinding-siteen_US
dc.subjectenzymatic-propertiesen_US
dc.subjectescherichia-colien_US
dc.subjecthuman salivaryen_US
dc.subjectgeneen_US
dc.subjectcalciumen_US
dc.subjectenzymesen_US
dc.titleIdentification of essential histidine residues in a recombinant alpha-amylase of thermophilic and alkaliphilic Bacillus sp strain TS-23en_US
dc.typeJournal Articlezh_TW
dc.identifier.doi10.1007/s00792-003-0341-8zh_TW
item.fulltextno fulltext-
item.languageiso639-1en_US-
item.openairetypeJournal Article-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.grantfulltextnone-
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