کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2078808 | 1545045 | 2008 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Purification and Properties of Cold-active Metalloprotease from Curtobacterium luteum and Effect of Culture Conditions on Production
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کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیوتکنولوژی یا زیستفناوری
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چکیده انگلیسی
Curtobacterium luteum, a gram-positive psychrotrophic bacterium, secreting an extracellular protease was isolated from the soil of Gangotri glacier, Western Himalaya. The maximum enzyme production was achieved when isolate was grown in a pH-neutral medium containing skim milk at 15°C over 120 hour. The metal ions such as Zn2+ and Cr2+ enhanced enzyme production. The specific activity of purified enzyme was 8090 u/mg after 34.1 fold purification. The 115 kD enzyme was a metalloprotease (activity inhibited by EDTA and EGTA) and showed maximum activity at 20°C and pH 7. The enzyme was active over a broad pH range and retained 84% of its original activity between pH 6-8. There was no loss in enzyme activity when exposed for 3 hours at 4°C-20°C. However, lost 65% of activity at 30°C, and was almost inactivated at 50°C, but was resistant to repeated freezing and thawing. The enzyme activity was stimulated by manganese ions; however, it was inactivated by copper ions.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chinese Journal of Biotechnology - Volume 24, Issue 12, December 2008, Pages 2074-2080
Journal: Chinese Journal of Biotechnology - Volume 24, Issue 12, December 2008, Pages 2074-2080
نویسندگان
Mohammed Kuddus, Pramod W. Ramteke,