DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, TU | ko |
dc.contributor.author | Gu, BG | ko |
dc.contributor.author | Jeong, YJ | ko |
dc.contributor.author | Shin,YC | ko |
dc.contributor.author | Byun, Si Myung | ko |
dc.date.accessioned | 2013-02-27T21:59:42Z | - |
dc.date.available | 2013-02-27T21:59:42Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1995-08 | - |
dc.identifier.citation | APPLIED AND ENVIRONMENTAL MICROBIOLOGY, v.61, no.8, pp.3105 - 3112 | - |
dc.identifier.issn | 0099-2240 | - |
dc.identifier.uri | http://hdl.handle.net/10203/71083 | - |
dc.description.abstract | An alkalophilic bacterium, Bacillus sp. strain GM8901, grown at pH 10.5 and 50 degrees C, produced five alkaline amylases in culture broth. At an early stage of the bacterial growth, amylase I (Amyl I) was produced initially and then, as cultivation progressed, four alkaline amylases, Amyl II, Amyl III, Amyl IV, and Amyl V, were produced from proteolytic degradation of Amyl I. A serine protease present in the culture medium was believed to be involved in Amyl I degradation, We purified Amyl I from the culture supernatant by ammonium sulfate precipitation, heparin-Sepharose CL-6B column chromatography, phenyl-Toyopearl column chromatography, and Mono Q HR5/5 high-performance liquid chromatography. The molecular weight of Amyl I was estimated to be about 97,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Amyl I had an extremely high optimal pH of 11.0 to 12.0 and was stable in a broad pH range of 6.0 to 13.0. Amyl I had an optimal temperature of 60 degrees C and was stable up to 50 degrees C. Thermostability was increased in the presence of Ca2+ and soluble starch. The enzyme required metal ions such as Ca2+, Mg2+, Cu2+, Co2+, Ag+, Zn2+, and Fe2+ for its enzyme activity and was inhibited by 1 mM EDTA and 1 mM phenylmethylsulfonyl fluoride. According to the mode of action of Amyl I on starch, Amyl I was classified as an alpha- and exo-amylase. Amyl I produced maltotetraose predominantly from starch via intermediates such as maltohexaose and maltopentaose. | - |
dc.language | English | - |
dc.publisher | AMER SOC MICROBIOLOGY | - |
dc.subject | PSEUDOMONAS-STUTZERI | - |
dc.subject | LICHENIFORMIS | - |
dc.title | PURIFICATION AND CHARACTERIZATION OF A MALTOTETRAOSE-FORMING ALKALINE ALPHA-AMYLASE FROM AN ALKALOPHILIC BACILLUS STRAIN, GM8901 | - |
dc.type | Article | - |
dc.identifier.wosid | A1995RM01500047 | - |
dc.type.rims | ART | - |
dc.citation.volume | 61 | - |
dc.citation.issue | 8 | - |
dc.citation.beginningpage | 3105 | - |
dc.citation.endingpage | 3112 | - |
dc.citation.publicationname | APPLIED AND ENVIRONMENTAL MICROBIOLOGY | - |
dc.contributor.nonIdAuthor | Kim, TU | - |
dc.contributor.nonIdAuthor | Gu, BG | - |
dc.contributor.nonIdAuthor | Jeong, YJ | - |
dc.contributor.nonIdAuthor | Shin,YC | - |
dc.description.isOpenAccess | N | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | PSEUDOMONAS-STUTZERI | - |
dc.subject.keywordPlus | LICHENIFORMIS | - |
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