Isolation, Purification and Characterization of a Thermophilic Alkaline Protease from Bacillus subtilis BP-36

نویسنده

  • E. Omidinia Pasteur Institute of Iran
چکیده مقاله:

The goal of this research was to isolate and identify the thermostable alkaline protease producing bacteria among several native Iranian microorganisms. At the end of screening program, a Bacillus subtilis BP-36 strain producing thermophilic alkaline protease was isolated from a hot spring in Ardebil province. The target enzyme was purified using a one-step Aqueous two-phase systems (ATPS) protocol involving 22% (w/w) polyethylene glycol (PEG)-10,000, and 18% (w/w) citrate with a yield of 39.7%, specific activity of 2600 U/mg and purification factor of 4.8. It was shown to have a molecular weight of 40 kDa by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The purified thermophile enzyme was stable in alkaline pH range (9.0-11.0) with the optimum pH of 9.0. It was highly stable at 60 °C and retained 100% activity even after 90 minutes, suggesting that it belong to the family of thermophilous. Collectively, our obtained data revealed that the thermophilic protease produced by B. subtilis BP-36 has the potential application in industrial processes under high temperature.

برای دانلود باید عضویت طلایی داشته باشید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

isolation, purification and characterization of a thermophilic alkaline protease from bacillus subtilis bp-36

the goal of this research was to isolate and identify the thermostable alkaline protease producing bacteria among several native iranian microorganisms. at the end of screening program, a bacillus subtilis bp-36 strain producing thermophilic alkaline protease was isolated from a hot spring in ardebil province. the target enzyme was purified using a one-step aqueous two-phase systems (atps) prot...

متن کامل

Cloning and Enhanced Expression of an Extracellular Alkaline Protease from a Soil Isolate of Bacillus clausii in Bacillus subtilis

in the detergent industry. In this study, the extracellular alkaline serine protease gene, aprE, from Bacillusclausii was amplified by PCR and further cloned and expressed in B. subtilis WB600 using the pWB980 expression vector. Protease activity of the recombinant B. subtilis WB600 harboring the plasmid pWB980/aprEreached up to 1020 U/ml, approximately 3-folds higher than the nativ...

متن کامل

Purification and Characterization of Alkaline Protease Produced by a Mutant Strain of Bacillus Subtilis

The present study describes the production, purification and characterization of alkaline protease from mutant strain of Bacillus subtilis EMS-8. The enzyme was purified using ammonium sulphate precipitation which gave 2.64 fold purification with 81.5% yield at 70% saturation. The molecular weight of the enzyme was determined using SDS-PAGE and it was found to be 25 KDa. The optimum pH of enzym...

متن کامل

cloning of alkaline protease gene from bacillus subtilis 168

the aim of this study was to clone the serine alkaline protease-encoding gene from bacillus subtilis 168. this protease, which can have many applications especially in detergent, may be industrially an important enzyme. for the amplification of the gene, pcr was performed with a pair of primers specifically designed for this purpose. electrophoresis of the pcr product showed the expected band o...

متن کامل

Isolation and purification of an extracellular protease from a new strain of Bacillus subtilis, viz.NCIM 2711.

A new extracellular protease having a prospective application in the food industry was isolated from Bacillus sUbtilis NCIM 2711 by (NH4)2SO4 precipitation from the cell broth. It was purified using DEAE-Cellulose and CM-Sephadex C-50 ion-exchange chromatography. With casein as a substrate, the proteolytic activity of the purified protease was found to be optimal at pH 7.0 and temperature 55 de...

متن کامل

منابع من

با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

ذخیره در منابع من قبلا به منابع من ذحیره شده

{@ msg_add @}


عنوان ژورنال

دوره 23  شماره 1

صفحات  7- 13

تاریخ انتشار 2012-03-01

با دنبال کردن یک ژورنال هنگامی که شماره جدید این ژورنال منتشر می شود به شما از طریق ایمیل اطلاع داده می شود.

میزبانی شده توسط پلتفرم ابری doprax.com

copyright © 2015-2023