Partial purification and characterization of cysteine proteinase inhibitor from chicken plasma |
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| Authors: | Rawdkuen Saroat Benjakul Soottawat Visessanguan Wonnop Lanier Tyre C |
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| Affiliation: | aDepartment of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, 90112, Thailand;bNational Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 113 Phaholyothin Rd., Klong1, Klong Luang, Pathumthani, 12120, Thailand;cDepartment of Food Science, North Carolina State University, Raleigh, NC 27695-7624, USA |
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| Abstract: | A high-molecular-weight cysteine proteinase inhibitor (CPI) was purified from chicken (Gallus gallus) plasma using polyethylene glycol (PEG) fractionation and affinity chromatography on carboxymethyl–papain–Sepharose-4B. The CPI was purified 96.8-fold with a yield of 28.9%. Based on inhibitory activity staining for papain, CPI was shown to have an apparent molecular mass of 122 kDa. No inhibitory activity was obtained under reducing condition, indicating that CPI from chicken plasma was stabilized by disulfide bonds. CPI was stable in temperature ranges from 40 to 70 °C for 10 min; however, more than 50% of the inhibitory activity towards papain was lost within 30 min of heating at 90 °C. CPI was stable in the presence of salt up to 3%. The purified CPI exhibited the inhibitory activity toward autolysis of arrowtooth flounder (Atheresthes stomias) and Pacific whiting (Merluccius productus) natural actomyosin (NAM) in a concentration-dependent manner. |
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| Keywords: | Autolysis Chicken plasma Cysteine proteinase inhibitor Purification |
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