کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
69734 48790 2014 7 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Improvement of P. aeruginosa 42A2 lipase preparations for FAMEs production, both in immobilized and soluble form
موضوعات مرتبط
مهندسی و علوم پایه مهندسی شیمی کاتالیزور
پیش نمایش صفحه اول مقاله
Improvement of P. aeruginosa 42A2 lipase preparations for FAMEs production, both in immobilized and soluble form
چکیده انگلیسی


• Soluble, cold-adapted lipases tested for the first time in biodiesel production.
• Vector and strain-based improved production of cold-adapted lipases LipC and LipCmut.
• Thermal resistance and methanol tolerance of soluble LipC and LipCmut preparations established.
• Soluble and immobilized cold-adapted LipC and LipCmut successfully assayed for FAMEs production.
• Milder conditions in biodiesel synthesis can lead to significant cost reductions and higher sustainability.

Lipase application in industrial biocatalytic processes is a topic of great interest due to their versatility and mild conditions of use. Many lipases from different sources have been studied, improved and used in a variety of chemical reactions. One of the most recent applications is the transesterification of vegetal triglycerides with methanol to produce fatty acid methyl esters (FAMEs), aimed at the synthesis of enzymatic biodiesel. In general, this process has been performed using immobilized lipases as biocatalysts. However, last tendencies are promoting the use of soluble enzyme preparations to reduce the cost of the enzymatic preparations and to make the whole process more competitive with respect to the chemical systems. In this work, we evaluated both, the soluble and immobilized preparations of two cold-adapted lipases: LipC from Pseudomonas aeruginosa 42A2, and its thermo stable variant LipCmut, which were over expressed and produced using a low cost protocol. Several conditions of soybean oil transesterification with such lipase preparations were tested to evaluate the enzymatic FAMEs production process.

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Molecular Catalysis B: Enzymatic - Volume 99, January 2014, Pages 1–7
نویسندگان
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