Expression of thermostable alkaline protease gene from Thermoactinomyces sp. E79 in E. coli and heat activation of the gene product

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dc.contributor.authorJung Kee Lee-
dc.contributor.authorYoung Ok Kim-
dc.contributor.authorK Sunitha-
dc.contributor.authorTae Kwang Oh-
dc.date.accessioned2017-04-19T08:55:37Z-
dc.date.available2017-04-19T08:55:37Z-
dc.date.issued1998-
dc.identifier.issn01415492-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/4521-
dc.description.abstractThe expression of Thermoactinomyces sp. E79 protease gene cloned into E. coli was highly host-dependent and the levels of protease expression was most stable in E. coli RR1 and E. coli HB101. Heating the intracellular extract at 70°C for 15 min converted the inactive recombinant E79 protease to its active mature form and also resulted in purification of the enzyme in a single step. Addition of 10 mM CaCl2 to the E79 protease decreased its autolysis and increased its thermal stability.-
dc.publisherSpringer-
dc.titleExpression of thermostable alkaline protease gene from Thermoactinomyces sp. E79 in E. coli and heat activation of the gene product-
dc.title.alternativeExpression of thermostable alkaline protease gene from Thermoactinomyces sp. E79 in E. coli and heat activation of the gene product-
dc.typeArticle-
dc.citation.titleBiotechnology Letters-
dc.citation.number9-
dc.citation.endPage840-
dc.citation.startPage837-
dc.citation.volume20-
dc.contributor.affiliatedAuthorTae Kwang Oh-
dc.contributor.alternativeName이정기-
dc.contributor.alternativeName김영옥-
dc.contributor.alternativeNameSunitha-
dc.contributor.alternativeName오태광-
dc.identifier.bibliographicCitationBiotechnology Letters, vol. 20, no. 9, pp. 837-840-
dc.identifier.doi10.1023/A:1005355324065-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Metabolic Regulation Research Center > 1. Journal Articles
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