کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8326780 | 1540196 | 2018 | 24 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Engineering and characterization of a novel low temperature active and thermo stable esterase from marine Enterobacter cloacae
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
Esterases are one of the most important industrial enzymes. Here, a novel estA was cloned from Enterobacter sp. and characterized. The sequence alignment results showed that it was a novel esterase. The purified EstA had a molecular weight of 26 KDa with an optimum temperature and pH of 40â¯Â°C and 9.0. EstA retained >70% activity between 0â¯Â°C and 20â¯Â°C, indicating it was a low temperature active enzyme. EstA exhibited low activity after incubation at 45â¯Â°C for 120â¯min or 50â¯Â°C for 30â¯min. In the presence of organic solvents, detergents and different concentrations of NaCl, EstA retained high activity. In order to improve thermal stability, a mutant A92D with better thermal stability than EstA was obtained by random mutation. ESTA92D showed high activity at 45â¯Â°C for 120â¯min and maintained 85% of the original activity at 50â¯Â°C for 30â¯min, approximately a 3.4-fold increase over EstA. Homology modeling analysis showed that the improved thermostability of ESTA92D was attributed to hydrophilic Asp rather than hydrophobic Ala, leading to an increase of the interaction and solubility as well as the surrounding area. The improved thermostability of low-temperature-active EstA suggests its immense applications in industrial applications.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 118, Part A, 15 October 2018, Pages 304-310
Journal: International Journal of Biological Macromolecules - Volume 118, Part A, 15 October 2018, Pages 304-310
نویسندگان
Mengmeng Ke, Bandikari Ramesh, Yian Hang, Ziduo Liu,