کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1189175 | 963507 | 2009 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and characterization of CEP from Lactococcus lactis ssp. lactis
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 112, Issue 3, 1 February 2009, Pages 533–538
Journal: Food Chemistry - Volume 112, Issue 3, 1 February 2009, Pages 533–538
نویسندگان
Yuxing Guo, Daodong Pan, Xiaoqun Zeng, Masaru Tanokura,