Abstract:
:Keratinase from Pseudomonas aeruginosa KS-1 was expressed constitutively as an extracellular protein in Escherichia coli with high specific activity of 3.7 kU/mg. It was purified fourfold as a 33 kDa monomeric protein by Q-Sepharose ion exchange chromatography with a recovery of 95%. It is a serine protease with optimal activity at pH 9 and 50°C. It was stable from pH 4 to 12 for 1 h with a t(1/2) of 12 min at 70°C. It hydrolyzed haemoglobin > fibrin > feather keratin > azo-casein > casein > meat protein > gelatin. Among synthetic substrates, it efficiently hydrolyzed N-Suc-ala-ala-pro-phe-pNA, N-Suc-ala-ala-ala-pNA, N-Suc-ala-ala-pro-leu-pNA and also plasmin substrate, D: -Val-Leu-Lys-pNA.
journal_name
Biotechnol Lettjournal_title
Biotechnology lettersauthors
Sharma R,Gupta Rdoi
10.1007/s10529-010-0361-2subject
Has Abstractpub_date
2010-12-01 00:00:00pages
1863-8issue
12eissn
0141-5492issn
1573-6776journal_volume
32pub_type
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doi:10.1007/s10529-012-0960-1
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journal_title:Biotechnology letters
pub_type: 杂志文章
doi:
更新日期:2003-12-01 00:00:00
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更新日期:2014-02-01 00:00:00