کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1187667 | 963470 | 2011 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Substrate specificities and mechanism of action of multiple α-galactosidases from Streptomyces griseoloalbus
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Substrate specificities and mechanism of action of multiple α-galactosidases from Streptomyces griseoloalbus Substrate specificities and mechanism of action of multiple α-galactosidases from Streptomyces griseoloalbus](/preview/png/1187667.png)
چکیده انگلیسی
α-Galactosidase or melibiase is a versatile enzyme with many potential biotechnological and industrial applications. The substrate specificities of three α-galactosidases – α-Gal I, α-Gal II, and α-Gal III – from Streptomyces griseoloalbus were studied using different galactose-containing natural substrates like melibiose, raffinose and stachyose. The kinetic parameters Km and Vmax were determined from the Lineweaver–Burk plot. α-Gal I showed highest affinity towards melibiose where as α-Gal II and α-Gal III showed highest affinity towards stachyose. The 1H NMR studies showed that all the three α-galactosidases had a retaining mechanism of hydrolysis.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 124, Issue 1, 1 January 2011, Pages 349–353
Journal: Food Chemistry - Volume 124, Issue 1, 1 January 2011, Pages 349–353
نویسندگان
G.S. Anisha, Rojan P. John, P. Prema,