کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
69294 48738 2016 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Biosynthesis of oleyl oleate in solvent-free system by Candida rugosa Lipase (CRL) immobilized in macroporous resin with cross-linking of aldehyde-dextran
ترجمه فارسی عنوان
بیوسنتز اولئات oleyl در سیستم بدون حلال توسط روگوزا لیپاز کاندیدا (CRL) بی حرکت در منافذ درشت رزین با اتصال عرضی آلدهید دکستران
کلمات کلیدی
بی‌حرکتی انعطاف پذیر؛ اولئات Oleyl؛ کاندیدا لیپاز روگوزا؛ سیستم حلال
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
چکیده انگلیسی


• Aldehyde-dextran was produced as flexible chain to immobilize Candida Rugosa Lipase.
• Lipase immobilized by flexible chain received higher activity recovery and stability.
• Enzymatic esterification of oleic acid and oleyl alcohol in solvent-free system was performed using immobilized Candida Rugosa Lipase, and received high conversion rate.

In our study, oleyl oleate was synthesized through enzymatic esterification of oleic acid with oleyl alcohol using Candida rugosa lipase (CRL) immobilized on macroporous resin in a solvent-free system. CRL was immobilized flexibly on the support via aldehyde-dextran, and the effectiveness of aldehyde-dextrans, as cross-linking agents with different molecular weights, was compared and discussed. The impact of various factors, such as different molecular weights of dextran, molar ratio between oleic acid and oleyl alcohol, and the temperature and stability of enzymes, on esterification was investigated as well. Our study indicated that lipase immobilized by 20000 Da dextran yielded the best result. The optimal condition to produce oleyl oleate using immobilized CRL was found in our study and turned out to be molar ratio of 1, reaction temperature of 40 °C, and a 12-h reaction time to reach reaction equilibrium. Under the optimal reaction conditions, a high percentage yield of ester was achieved (92.6%). The immobilized CRL also reached a conversion rate of 86.7% with excellent stability even after 8 cycles.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 133, November 2016, Pages 1–5
نویسندگان
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