Extracellular expression of keratinase Ker P from Pseudomonas aeruginosa in E. coli.

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 Lett

journal_title

Biotechnology letters

authors

Sharma R,Gupta R

doi

10.1007/s10529-010-0361-2

subject

Has Abstract

pub_date

2010-12-01 00:00:00

pages

1863-8

issue

12

eissn

0141-5492

issn

1573-6776

journal_volume

32

pub_type

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