کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
7790556 1500643 2015 11 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Mode of action of Bacillus licheniformis pectin methylesterase on highly methylesterified and acetylated pectins
ترجمه فارسی عنوان
نحوه عمل پکتین متیل استراز باسیلوس لیفتینوفیسسیس بر پکتین های بسیار متیل استرالیتی و آکسیلت شده
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آلی
چکیده انگلیسی
A gene encoding a putative pectinesterase from Bacillus licheniformis DSM13 was cloned and expressed in Escherichia coli. The resulting recombinant enzyme (BliPME) was purified and characterized as a pectin methylesterase. The enzyme showed maximum activity at pH 8.0 and 50 °C. BliPME is able to release up to 100% of the methylesters from lime pectin (DM 34-76 → DM 0) and up to 73% of all methylesters from SBPs (DM 30-73 → DM 14). BliPME efficiently de-methylesterifies lemon pectins and SBPs in a blockwise manner and is quite tolerant towards the acetyl groups present within the SBPs. Detailed analysis of the BliPME-modified pectins using HILIC-MSn and the classical calcium reactivity measurement showed that the enzyme generates pectins with low methylesterification (lime and SBP) and high acetyl content (SBP) while creating blocks of nonmethylesterified galacturonic acid residues. The high activity of BliPME towards highly methylesterified and acetylated pectins makes this novel esterase more efficient in removing methylesters from highly esterified beet pectin compared to other PMEs, e.g. Aspergillus niger PME.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Carbohydrate Polymers - Volume 115, 22 January 2015, Pages 540-550
نویسندگان
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