کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
69838 48795 2014 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Aldehydepropyl-functionalized mesostructured cellular foams: Efficient supports for immobilization of penicillin G acylase
ترجمه فارسی عنوان
فویل سلولهای مزودستروپلییل-عاملدهنده آلدهیدپروپیل: پشتیبانی های کارآمد برای بی تحرکی پنی سیلین گلیکول
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
چکیده انگلیسی


• CHO-MCFs were prepared by post-synthetical functionalization of MCFs.
• The aldehydepropyl groups were grafted successfully on the surface of CHO-MCFs.
• The ultra-large 3D mesostructure of CHO-MCFs is beneficial for immobilization of PGA.
• PGA immobilized covalently on CHO-MCFs increased the operational stability.

The aldehydepropyl-functionalized mesostructured cellular foams (CHO-MCFs) were prepared by post-synthetical functionalization of MCFs with trimethoxysilylpropanal (TMSP), and used as efficient supports for immobilization of penicillin G acylase (PGA). The physicochemical properties of CHO-MCFs were characterized by SAXS, nitrogen sorption, TEM, elementary analysis, solid state 29Si MAS NMR, FT-IR spectroscopy and thermogravimetry. The results show that the aldehydepropyl groups have been grafted successfully on the surface of MCFs, and after functionalization, the BET surface area and pore volume of CHO-MCFs decrease, but the ultra-large and continuous 3D mesoporous structure of CHO-MCFs are retained to be beneficial for immobilization of PGA with large size and diffusion of substrates and products. PGA is immobilized covalently on CHO-MCFs via the reaction to produce Schiff's base between the free amino groups of lysine residues of PGA and the aldehyde groups on the surface of CHO-MCFs, which greatly increases the operational stability of the immobilized PGA with little activity loss due to the short-chain groups of aldehydepropyl grafted on the surface of CHO-MCFs. PGA/CHO-MCFs-10 shows the immobilization yield of 57.6%, the specific activity of 22.2 U/mg and the initial enzymatic activity of 8895 U/g, and retains 93.0% of its initial enzymatic activity after recycled for 10 times.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 105, July 2014, Pages 111–117
نویسندگان
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