کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
70320 48822 2011 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Optimized enzymatic synthesis of ascorbyl esters from lard using Novozym 435 in co-solvent mixtures
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
پیش نمایش صفحه اول مقاله
Optimized enzymatic synthesis of ascorbyl esters from lard using Novozym 435 in co-solvent mixtures
چکیده انگلیسی

A mild and efficient method for the conversion of fatty acid methyl esters from lard into ascorbyl esters via lipase-catalyzed transesterification in co-solvent mixture is described. A solvent engineering strategy was firstly applied to improve fatty acid ascorbyl esters production. The co-solvent mixture of 30% t-pentanol:70% isooctane (v/v) was optimal. Response surface methodology (RSM) and central composite design (CCD) were employed to estimate the effects of reaction parameters, such as reaction time (12–36 h), temperature (45–65 °C), enzyme amount (10–20%, w/w, of fat acid methyl esters), and substrate molar ratio of fatty acid methyl esters to ascorbic acid (8:1–12:1) for the synthesis of fatty acid ascorbyl esters in co-solvent mixture. Based on the RSM analysis, the optimal reaction conditions were determined as follows: reaction time 34.32 h, temperature 54.6 °C, enzyme amount 12.5%, substrate molar ratio 10.22:1 and the maximum conversion of fatty acid ascorbyl esters was 69.18%. The method proved to be applicable for the synthesis of ascorbyl esters using Novozym 435 in solvent.

Lipase-catalyzed transesterification of ascorbic acid and methyl esters of lard using immobilized Novozym 435 in co-solvent mixture.Figure optionsDownload as PowerPoint slideResearch highlights
► Lipase-catalyzed transesterification of ascorbic acid and methyl esters of lard were conducted using immobilized Novozym 435 in solvent system.
► A co-solvent mixture was used to synthesize ascorbyl esters.
► Response surface methodology was used to optimize the transesterification.
► The optimal reaction conditions were obtained through RSM.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 69, Issues 3–4, May 2011, Pages 107–111
نویسندگان
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