Effect of temperature , pH , substrate ( Starch ) and glucose on stability of α - amylase from Bacillus licheniformis ATCC 6346

نویسنده

  • Vasanthy Arasaratnam
چکیده

Thermostable α-amylases (1,4-α-D-glucan glucanohydrolase; E.C.3.2.1.1) from Bacillus species are of great industrial importance in the production of corn syrup or dextrose. The present study was aimed to determine the effect of temperature, pH, substrate and glucose on stability of α-amylase from Bacillus licheniformis ATCC 6346. To determine the effect of temperature and pH on the stability of α-amylase this was pre-incubated at different temperatures and pHs. The enzyme pre-incubated with starch and glucose separately at 85C to determine the effect of substrate and endproduct on the stability of α-amylase. Crude -amylase retained 60% of the original activity when it was pre-incubated at 85C for 10 min. This enzyme was more stable at pH 9.0 than other pH values (7.0 and 8.0) and no significant important was observed with addition of substrate (starch). Presence of glucose slightly increased the stability of -amylase. There was no significant improvement in the stability of -amylase was observed with the addition of starch however presence of glucose slightly increased the stability of the α-amylase.

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

Comparative study on production of a-Amylase from Bacillus licheniformis strains

Alpha amylase (α-1, 4-glucan-glucanhydrolase, EC 3.2.1.1), an extracellular enzyme, degrades α, 1-4 glucosidic linkages of starch and related substrates in an endo-fashion producing oligosaccharides including maltose, glucose and alpha limit dextrin (7). The present study deals with the production and comparative study of production of α-amylase from two strains of Bacillus licheniformis, MTCC ...

متن کامل

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

Single Step Purification of Novel Thermostable and Chelator Resistant Amylase from Bacillus Licheniformis RM44 by Affinity Chromatography

Bacillus licheniformis RM44 was isolated from hot spring near Karachi and screened forthe production of extracellular amylase Amy RM44. Amy RM44 was purified to homogeneityon a single step by affinity chromatography using insoluble corn starch. The molecular weightof Amy RM44 was estimated to be 66 kDa by SDS–PAGE and zymographic analysis. Nine foldpurification was achieved with the specific ac...

متن کامل

Purification and Characterization of a Novel Thermostable and Acid Stable α-Amylase from Bacillus Sp. Iranian S1

This study reports the purification and biochemical characterization of thermostable and acidic-pH-stable α-amylase from Bacillus sp. Iranian S1 isolated from the desert soil (Gandom-e-Beryan in Lut desert, Iran). Amylase production was found to be growth associated. Maximum enzyme production was in exponential phase with activity 2.93 U ml-1 at 50°C and pH 5. The enzyme was purified by isoprop...

متن کامل

Single Step Purification of Novel Thermostable and Chelator Resistant Amylase from Bacillus Licheniformis RM44 by Affinity Chromatography

Bacillus licheniformis RM44 was isolated from hot spring near Karachi and screened forthe production of extracellular amylase Amy RM44. Amy RM44 was purified to homogeneityon a single step by affinity chromatography using insoluble corn starch. The molecular weightof Amy RM44 was estimated to be 66 kDa by SDS–PAGE and zymographic analysis. Nine foldpurification was achieved with the specific ac...

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 2014