کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5511629 | 1540214 | 2017 | 38 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Recombinant thermo-alkali-stable endoglucanase of Myceliopthora thermophila BJA (rMt-egl): Biochemical characteristics and applicability in enzymatic saccharification of agro-residues
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Codon adaptation index (CAI) of a 1263 bp long endoglucanase encoding gene from the thermophilic mould Myceliopthora thermophile BJA has been improved from 0.44 to 0.76 by in vitro gene synthesis. The codon optimized endoglucanase gene (Mt-egl) has been constitutively expressed in Pichia pastoris under the regulation of GAP promoter. Recombinant endoglucanase (rMt-egl), purified by size exclusion chromatography, has been confirmed to be a monomeric protein of â¼47 kDa. rMt-egl is optimally active at pH 10 and 50 °C, displaying stability in broad pH and temperature ranges, with a t1/2 of 60 and 15 min at 90 and 100 °C, respectively. This retained â¼70% of activity after 3 h incubation at pH 5-12. The Km, Vmax, kcat and kcat/Km of rMt-egl were 5 mg mLâ1, 20 μmoles minâ1 mgâ1, 1.02 Ã 103 sâ1 and 204 sâ1 mgâ1 mLâ1, respectively. Homology modeling and bioinformatics analysis confirmed catalytically important role of glutamate 234 and 344. rMt-egl released high amounts of reducing sugars from wheat bran and corn cobs (421 and 382 mg gâ1), thus making it a useful biocatalyst for producing bioethanol and fine chemicals from agro-residues.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 104, Part A, November 2017, Pages 107-116
Journal: International Journal of Biological Macromolecules - Volume 104, Part A, November 2017, Pages 107-116
نویسندگان
Priya Phadtare, Swati Joshi, T. Satyanarayana,