کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10235290 | 45028 | 2014 | 8 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Highly thermostable carbonic anhydrase from Persephonella marina EX-H1: Its expression and characterization for CO2-sequestration applications
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موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
بیو مهندسی (مهندسی زیستی)
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چکیده انگلیسی
The codon-optimized carbonic anhydrase gene of Persephonella marina EX-H1 (PMCA) was expressed and characterized. The gene with the signal peptide removed, PMCA(spâ), resulted in the production of approximately five times more purified protein than from the intact gene PMCA using an Escherichia coli expression system. PMCA(spâ) is formed as homo-dimer complex. PMCA(spâ) has a wide pH tolerance (optimum pH 7.5) and a high thermostability even at 100 °C (88 min of thermal deactivation half-life). The melting temperature for PMCA(spâ) was 84.5 °C. The apparent kcat and Km values for CO2 hydration were 3.2 Ã 105 sâ1 and 10.8 mM. The activity of the PMCA(spâ) enzyme was enhanced by Zn2+, Co2+, and Mg2+, but was strongly inhibited by Cu2+, Fe3+, Al3+, Pb2+, Ag+, and Hg2+. PMCA(spâ) readily catalyzed the hydration of CO2, precipitating CaCO3 as calcite in the presence of Ca2+.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Process Biochemistry - Volume 49, Issue 12, December 2014, Pages 2114-2121
Journal: Process Biochemistry - Volume 49, Issue 12, December 2014, Pages 2114-2121
نویسندگان
Bashistha Kumar Kanth, So-Young Jun, Shipra Kumari, Seung Pil Pack,