کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10541804 | 963435 | 2011 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Enzymatic properties and transglycosylation of α-galactosidase from Penicillium oxalicum SO
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: Enzymatic properties and transglycosylation of α-galactosidase from Penicillium oxalicum SO Enzymatic properties and transglycosylation of α-galactosidase from Penicillium oxalicum SO](/preview/png/10541804.png)
چکیده انگلیسی
Penicillium oxalicum SO α-galactosidase demonstrated weak hydrolysing activity but a high rate of transglycosylation in the reaction with melibiose, where the major product was 6-α-galactosyl melibiose. The transfer ratio was 83.6% and was maintained over a long reaction time of 80 h. The molecular weight was estimated to be 124,000 by SDS-PAGE. The optimal pH was â¼3 and a stable pH, with a range of 2.4-9.5, was found. The optimal temperature was â¼60 °C and the activity was stable below 60 °C. With respect to acceptor specificity, mono-alcohols, sugar alcohols and sugars were poor acceptors, but the di-alcohol ethylene glycol and the tri-alcohol glycerin were good acceptors. The percentage of transglycosylation to glycerin increased up to 41.7%, as that to melibiose decreased, with the initial glycerin concentration of 40%. The production of α-d-galactosylglycerol was 293 mg for each gram of melibiose used by the enzymatic reaction.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 126, Issue 1, 1 May 2011, Pages 177-182
Journal: Food Chemistry - Volume 126, Issue 1, 1 May 2011, Pages 177-182
نویسندگان
Masahiro Kurakake, Youichirou Moriyama, Riku Sunouchi, Shinya Nakatani,