Purification and characterization of a collagenolytic serine proteinase from the skeletal muscle of red sea bream (Pagrus major) |
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| Authors: | Guo-Ping Wu Su-Hua Chen Guang-Ming Liu Asami Yoshida Ling-Jing Zhang Wen-Jin Su Min-Jie Cao |
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| Affiliation: | 1. Fisheries College, The Key Laboratory of Science and Technology for Aquaculture and Food Safety, Jimei University, Xiamen 361021, China;2. School of Environmental and Chemical Engineering, Nanchang Hangkong University, Nanchang 330063, China;3. College of Biological Engineering, Jimei University, Jimei, Xiamen 361021, China;4. Graduate School of Science and Technology, Nagasaki University, Nagasaki 852-8521, Japan |
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| Abstract: | A collagenolytic serine proteinase (CSP) was purified from red sea bream (Pagrus major) skeletal muscle to homogeneity by ammonium sulfate fractionation and chromatographies including DEAE-Sephacel, Phenyl Sepharose and Hydroxyapatite. The molecular mass of CSP was approximately 85 kDa as estimated by SDS–PAGE and gel filtration. Optimum temperature and pH of CSP were 40 °C and 8.0, respectively. CSP was specifically inhibited by serine proteinase inhibitors, while inhibitors to other type proteinases did not show much inhibitory effects. The Km and kcat values of CSP for Boc-Leu-Lys-Arg-MCA were 3.58 µM and 0.13 s? 1 at 37 °C, respectively. Furthermore, CSP hydrolyzed gelatin and native type I collagen effectively though its degradation on myosin heavy chain (MHC) was not significant, suggesting its involvement in the texture tenderization of fish muscle during the post-mortem stage. |
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