Purification and characterization of CEP from Lactococcus lactis ssp. lactis |
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Authors: | Yuxing Guo Daodong Pan Xiaoqun Zeng Masaru Tanokura |
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Affiliation: | 1. Food Science & Nutrition Department of Nanjing Normal University, Nanjing 210097, PR China;2. Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Science, University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-8657, Japan |
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Abstract: | The cell-envelope proteinase (CEP) of Lactococcus lactis ssp. lactis LB12 was released from cells by treatment with lysozyme, purified by ammonium sulfate precipitation and chromatographed on DEAE-Sephadex A-25 and Sephacryl S-300 HR. The purified CEP is a monomer structure and has molecular mass of about 53 kDa. Optimal activity occurred at pH 7.5 and 40 °C. It is a metallopeptidase, activated by Mn2+, Mg2+, Ca2+, inhibited by Co2+, Zn2+, Ni2+ and EDTA, and a serine proteinase which is inhibited by PMSF. The sequence of the first 13 amino acids of the N-terminal of the CEP was determined to be Asp-Val-Phe-Ala-Pro-His-Met-Ala-Asn-Val-Ala-Ala-Val, and the whey protein hydrolysate produced by the CEP displayed ACE-inhibitory activity. |
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Keywords: | CEP Purification and characterization Whey protein hydrolysate ACE-inhibitory activity |
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