Production, Partial Purification and Proteolysis of Carboxymethylcellulases from Arachniotus citrinus

نویسنده

  • A. JABBAR
چکیده

Carboxymethylcellulases (CMCases) of Arachniotus citrinus were produced under solid state fermentation on different carbon sources including wheat bran, corn cob, alkali treated corn cob and mixture of wheat bran and alkali treated corn cob at 30C for 15 days. In this case, mixture of wheat bran and corn cob was observed to be the best carbon source as maximum specific activity (4.2 U mg proteins) for crude CMCases was obtained on it. CMCases were partially purified by ammonium sulphate precipitation. The onset of CMCases precipitation occurred at 35% and completed at 75% saturation of ammonium sulphate at 0C. The purification after ammonium sulphate precipitation was 1.72-fold while 86% CMCases were recovered. After dialysis, specific activity of CMCases was 7.29 U mg. CMCases were found resistant against chymotrypsin and subtilisin as residual activity of CMCases against these proteases was 85 and 70% after 70 min, respectively.

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Two-step purification and partial characterization of an extra cellular α-amylase from Bacillus licheniformis

The aim of this study was production and partial purification of α-amylase enzyme by Bacillus licheniformis. B. Licheniformis was allowed to grow in broth culture for purpose of inducing α-amylase enzyme. Optimal conditions for amylase production by B. Licheniformis are incubation period of 120 h, temperature of 37 °C and pH 7.0. The α-amylase enzyme was purified by ion exchange chromatography ...

متن کامل

Purification and Partial Characterization of a Thrombin-Like Enzyme (AH144) from Venom of Iranian Snake Agkistrodon Halys

The snake venom´s thrombin-like enzymes comprise a number of serine proteases, which are functionally and structurally related to thrombin. Purification and partial characterization of a thrombin-like enzyme from the venom of the Iranian snake, Agkistrodon halys, was the aim of this study. Purification was carried out by a combination of variety of chromatographic methods that included: gel...

متن کامل

Partial Purification of a Potent Immunosuppressive Factor Excreted from Leishmania major Promastigote and Amastigote

Recent scientific evidence indicates that distinct patterns of susceptibility in BALB/c mice to Leishmania major infection are attributable to the differential expansion of distinct CD4+ T-cell subsets and their cytokines production. Production of the Th1 cytokine IFN-g is associated with resistance, whereas production of the Th2 cytokines IL-4 and IL-10 are associated with extreme susceptibili...

متن کامل

Partial Purification and Characterization of Anticoagulant Factor from the Snake (Echis carinatus) Venom

  Objective(s): Snake venoms contain complex mixture of proteins with biological activities. Some of these proteins affect blood coagulation and platelet function in different ways. Snake venom toxin may serve as a starting material for drug design to combat several pathophysiological problems such as cardiovascular disorders. In the present study, purification of anticoagulation facto...

متن کامل

Production and partial purification of thermostable bacteriocins from Bacillus pumilus ZED17 and DFAR8 strains with antifungal activity

The bacteria which are members of the genus Bacillus are known to produce a wide variety of antimicrobial substances and bacteriocins. The main objective of this study was to investigate the effect of these bacteriocins on eukaryotic cells such as fungi, yeast and plant seeds. Several strains were screened for antifungal activities and identified by the means of polymerase chain reacti...

متن کامل

ذخیره در منابع من


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

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

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2008