کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1987882 1540312 2008 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Immobilization of trypsin on chitosan gels: Use of different activation protocols and comparison with other supports
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Immobilization of trypsin on chitosan gels: Use of different activation protocols and comparison with other supports
چکیده انگلیسی

Trypsin was immobilized on chitosan gels coagulated with 0.1 or 1 M NaOH and activated with glutaraldehyde or glycidol. The derivatives were characterized by their recovered activity, thermal (40, 55 and 70 °C) and alkaline (pH 11) stabilities, amount of enzyme immobilized on gels for several enzyme loads (8–14 mgprotein/gGel) and compared to agarose derivatives. Enzyme loads higher than 14 mgprotein/gGel can be immobilized on glutaraldehyde derivatives, which showed 100% immobilization yield and, for loads up to 8 mgprotein/gGel, 100% recovered activity. Activation with glycidol led to lower immobilization yields than the ones obtained with glutaraldehyde, 61% for agarose-glyoxyl (AgGly) with low grade of activation and 16% for the chitosan-glyoxyl (ChGly), but allowed obtaining the most stable derivative (ChGly), that was 660-fold more stable than the soluble enzyme at 55 and 70 °C—approximately threefold more stable than AgGly. The ChGly derivative presented also the highest stability during incubation at pH 11. Analyses of lysine residue contents in soluble and immobilized trypsin indicated formation of multipoint bonds between enzyme and support, for glyoxyl derivatives.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 43, Issue 1, 1 July 2008, Pages 54–61
نویسندگان
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