کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5412997 | 1506613 | 2010 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Immobilization of β-galactosidase onto Sepharose and stabilization in room temperature ionic liquids
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The hydrolysis of o-nitrophenyl-β-d-galactopyranoside (ONPG) by β-galactosidase immobilized on Sepharose CL-4B® was investigated in five different ionic liquids (ILs), 1-butyl-3-methylimidazolium Xâ; [X = CF3SO3â, BF4â, PF6â, CH3SO4âand N(CN)2â]. Michaelis-Menten kinetic studies were conducted in phosphate buffer and in the five ionic liquids. For the immobilized enzyme in the ILs, the Km values were lower (0.36-1.2 mmol ONPG) while the Vmax values were higher (0.04-0.008 minâ 1) compared to those in aqueous phosphate buffer suggesting a marked increase in the efficiency of the immobilized enzyme in the ionic liquid. For the free enzyme in the ionic liquids, the Km values, in general, were larger (0.45-4.96 mmol ONPG) than those of the immobilized enzyme in the ionic liquid. A postulated mechanism for the hydrolysis is suggested, involving interception of the intermediate oxonium ion species by the counter ion of the ionic liquid, thereby enabling the hydrolysis to occur at a faster rate.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Liquids - Volume 152, Issues 1â3, 15 March 2010, Pages 19-27
Journal: Journal of Molecular Liquids - Volume 152, Issues 1â3, 15 March 2010, Pages 19-27
نویسندگان
Natasha R. Singh, Dyer Narinesingh, Gurdial Singh,