کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
4754892 | 1361490 | 2017 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Exploring substrate specificities of a recombinant Rhizopus oryzae lipase in biodiesel synthesis
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The alcoholysis of triolein was used to explore the specific features of a recombinant Rhizopus oryzae lipase (rROL) for biodiesel synthesis. For this purpose, different acylglycerols were compared as substrates in lipase-catalysed transesterification. rROL was shown to exhibit a higher specificity towards 1-monoolein than triolein compared to other R. oryzae lipases, being more than 4-fold more specific; in contrast, rROL did not accept 2-monoolein as substrate, concluding that it is highly 1,3-positional specific. Comparing ethanol and methanol as acyl-acceptors, it was observed that the latter caused more lipase inactivation. Regarding alcohols, it was also demonstrated that acyl migration occurred in moderate alcohol concentrations.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: New Biotechnology - Volume 39, Part A, 25 October 2017, Pages 59-67
Journal: New Biotechnology - Volume 39, Part A, 25 October 2017, Pages 59-67
نویسندگان
Albert Canet, M. Dolors Benaiges, Francisco Valero, Patrick Adlercreutz,