Enzymatic evaluation of Bacillus amyloliquefaciens phytase as a feed additive

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dc.contributor.authorDong Hyun Kim-
dc.contributor.authorByung Chul Oh-
dc.contributor.authorWon Chan Choi-
dc.contributor.authorJung Kee Lee-
dc.contributor.authorTae Kwang Oh-
dc.date.accessioned2017-04-19T08:56:42Z-
dc.date.available2017-04-19T08:56:42Z-
dc.date.issued1999-
dc.identifier.issn0141-5492-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4951-
dc.description.abstractPhytases from Bacillus amyloliquefaciens DS11 and Aspergillus ficuum for feed enzyme were compared on the basis of phosphate inhibition and thermal stabilities. The apparent half-life of the former enzyme at 80 °C was 42 min. The activity of B. amyloliquefaciens phytase was retained up to 5 mM phosphate while 3 mM phosphate inhibited 50% of the original activity in case of A. ficuum phytase. Addition of 5 mM CaCl2 significantly broadened the active pH range and also increased the pH stability of DS11 phytase.-
dc.publisherSpringer-
dc.titleEnzymatic evaluation of Bacillus amyloliquefaciens phytase as a feed additive-
dc.title.alternativeEnzymatic evaluation of Bacillus amyloliquefaciens phytase as a feed additive-
dc.typeArticle-
dc.citation.titleBiotechnology Letters-
dc.citation.number0-
dc.citation.endPage927-
dc.citation.startPage925-
dc.citation.volume21-
dc.contributor.affiliatedAuthorDong Hyun Kim-
dc.contributor.affiliatedAuthorByung Chul Oh-
dc.contributor.affiliatedAuthorWon Chan Choi-
dc.contributor.affiliatedAuthorJung Kee Lee-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.alternativeName김동현-
dc.contributor.alternativeName오병철-
dc.contributor.alternativeName최원찬-
dc.contributor.alternativeName이정기-
dc.contributor.alternativeName오태광-
dc.identifier.bibliographicCitationBiotechnology Letters, vol. 21, pp. 925-927-
dc.identifier.doi10.1023/A:1005602717835-
dc.subject.keywordcalcium-
dc.subject.keywordpH stability-
dc.subject.keywordphosphate inhibition-
dc.subject.keywordphytase-
dc.subject.keywordthermal stability-
dc.subject.localcalcium-
dc.subject.localCalcium-
dc.subject.localpH stability-
dc.subject.localphosphate inhibition-
dc.subject.localphytase-
dc.subject.localPhytase-
dc.subject.localthermal stability-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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