Abstract:
:Pseudomonas fluorescens RO98, a raw milk isolate, was inoculated into McKellar's minimal salts medium and incubated at 25 degrees C for 48 h to allow production of protease. A zinc-metalloacid protease was purified from the cell-free concentrate by anion exchange and gel filtration chromatography. The purified protease was active between 15 and 55 degrees C, and pH 4.5 and 9.0, and was stable to pasteurization. The enzyme had pH and temperature optima for activity of 5.0 and 35 degrees C, respectively. It was heat stable with a D55 of 41 min and a D62.5 of 18 h. Molecular weight of the enzyme was estimated to be 52 kDa by SDS PAGE and size exclusion chromatography. Values for kM of 144.28, 18.73, 110.20 and 35.23 micromol were obtained for whole, alpha-, beta- and kappa-casein, with a Vmax of 8.26, 0.09, 0.42 and 0.70 micromol mg-1 min-1, respectively. The enzyme hydrolysed kappa-casein preferentially when incubated with artificial casein micelles.
journal_name
J Appl Microbioljournal_title
Journal of applied microbiologyauthors
Koka R,Weimer BCdoi
10.1046/j.1365-2672.2000.01108.xsubject
Has Abstractpub_date
2000-08-01 00:00:00pages
280-8issue
2eissn
1364-5072issn
1365-2672pii
jam1108journal_volume
89pub_type
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journal_title:Journal of applied microbiology
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更新日期:2012-12-01 00:00:00
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journal_title:Journal of applied microbiology
pub_type: 杂志文章,评审
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journal_title:Journal of applied microbiology
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journal_title:Journal of applied microbiology
pub_type: 杂志文章
doi:10.1046/j.1365-2672.1999.00701.x
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journal_title:Journal of applied microbiology
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doi:10.1046/j.1365-2672.1999.00845.x
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journal_title:Journal of applied microbiology
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更新日期:1998-01-01 00:00:00
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更新日期:1998-06-01 00:00:00
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更新日期:2021-01-01 00:00:00