نتایج جستجو برای: alkaline serine protease

تعداد نتایج: 118515  

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...

Journal: :biomacromolecular journal 0
tayebeh nazari department of bioscience and biotechnology, malek-ashtar university of technology, tehran, iran mahdi alijanianzadeh department of bioscience and biotechnology, malek ashtar university of technology, tehran, iran ahmad molaeirad department of bioscience and biotechnology, malek-ashtar university of technology, tehran, iran maryam khayati department of bioscience and biotechnology, malek-ashtar university of technology, tehran, iran

proteases are important enzymes that their role in various industries is undeniable. however, keeping enzymes stable during its activity in harsh conditions is so important. in this study, protease enzyme was immobilized on the porous silica particles and its stability in different temperatures and phs was evaluated. first silica particles were aminated by 3-aminopropyltriethoxysilane then the ...

Background: Alkaline proteases is the important group of enzymes having numerous industrial applications including dairy food formulations. Objectives: The current study deals with the purification and characterization of an alkaline serine protease produced by Geotrichum candidum QAUGC01, isolated from indigenous fermented milk product, Dahi.<br...

Journal: :research in pharmaceutical sciences 0
h mir mohammad sadeghi m rabbani m naghitorabi

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...

Journal: :International journal of food microbiology 2014
Houda Banani Davide Spadaro Dianpeng Zhang Slavica Matic Angelo Garibaldi Maria Lodovica Gullino

The yeast-like fungus Aureobasidium pullulans PL5 is a microbial antagonist against postharvest pathogens of fruits. The strain is able to produce hydrolases, including glucanases, chitinases and proteases. The alkaline serine protease gene ALP5 from A. pullulans was cloned, inserted into the vector pPIC9 to construct pPIC9/ALP5, and then expressed in Pichia pastoris strain KM71. ALP5 had a mol...

Journal: :Preparative biochemistry & biotechnology 2009
Dilek Kazan Hulya Bal Aziz Akin Denizci Nurcin Celik Ozturk Hasan Umit Ozturk Aydan Salman Dilgimen Dilek Coskuner Ozturk Altan Erarslan

An alkali tolerant Bacillus strain having extracellular serine alkaline protease activity was newly isolated from compost and identified as Bacillus clausii GMBE 22. An alkaline protease (AP22) was 4.66-fold purified in 51.5% yield from Bacillus clausii GMBE 22 by ethanol precipitation and DEAE-cellulose anion exchange chromatography. The purified enzyme was identified as serine protease by LC-...

Journal: :iranian journal of biotechnology 2008
sara seifzadeh reza hassan sajedi reyhaneh sariri

thermophilic bacillus sp. gus1, isolated from  a soil  sample obtained from citrus garden, produced at least three proteases as detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis (sds-page) and zymogram analysis. the enzymes were stable in the alkaline ph range (8.0-12.0), with the optimum temperature and ph range of the proteases being 70ºc and 6.0-12.0, respectively. all th...

Journal: :Acta Crystallographica Section A Foundations of Crystallography 1993

Journal: :Bioscience, biotechnology, and biochemistry 2006
Endang Setyorini Shinji Takenaka Shuichiro Murakami Kenji Aoki

Bacillus subtilis strain FP-133, isolated from a fermented fish paste, synthesized two novel halotolerant extracellular proteases (expro-I and expro-II), showing activity and stability at concentrations of 0-20% (w/v) NaCl. Each protease was purified to homogeneity and characterized. The purified expro-I was a non-alkaline serine protease with an optimum pH of 7.5, although most serine protease...

Journal: :Agricultural and biological chemistry 1991
H Shimogaki K Takeuchi T Nishino M Ohdera T Kudo K Ohba M Iwama M Irie

In the course of a search for an alkaline stable protease for industrial use, an alkaline protease (protease BYA) was isolated from an alkalophilic Bacillus sp. Y, and its properties were characterized. Its optimum pH was pH 10.0-12.5, when casein was used as a substrate. In addition to the stability of protease BYA at pH 6.5-13.0, it was also very stable towards various surface-active agents, ...

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