کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1987514 1540295 2010 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
A novel thermostable, acidophilic α-amylase from a new thermophilic “Bacillus sp. Ferdowsicous” isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
A novel thermostable, acidophilic α-amylase from a new thermophilic “Bacillus sp. Ferdowsicous” isolated from Ferdows hot mineral spring in Iran: Purification and biochemical characterization
چکیده انگلیسی

This paper describes the purification and characterization of a novel acidophile α-amylase from newly isolated Bacillus sp. Ferdowsicous. The enzyme displayed a molecular weight of 53 kDa and it was stable over a range of pH from 3.5 to 7 with an optimum around 4.5. The optimum temperature for activity was found to be around 70 °C and the enzyme remained active to more than 75% up to 75 °C for 45 min. The enzyme activity was decreased by Zn2+and EDTA but inhibited by Hg2+, whereas the activity was increased by approximately 15% by Ba2+ and Fe2+. Na+, Mg2+, K+, Ca2+, PMSF, Triton X-100 and β-mercaptoethanol had any considerable effect on its activity. The enzyme activity on the amylose as substrate was 1.98 times greater than amylopectin. Partial N-terminal sequencing demonstrated no significant similarity with other known α-amylases, indicating that the presented enzyme was new. Considering its promising properties, this enzyme can find potential applications in the food industry as well as in laundry detergents.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 46, Issue 3, 1 April 2010, Pages 289–297
نویسندگان
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