Purification and Characterization of Α-amylase Produced by Aspergillus Niger Using Banana Peels

نویسنده

  • KIRAN KUMAR
چکیده

The present study was aimed at purification and characterization of α-amylase enzyme from strain of Aspergillus niger isolated from local soil samples. Solid state fermentation (SSF) was carried out to produce α-amylase from A. niger using waste banana peel as substrate. The maximum activity of α-amylase (11926 U/gds) was recorded after 72 hours of fermentation. The extracted enzyme was subjected to purification by ammonium sulphate precipitation, sephadex G-100 gel and through ion exchange chromatography. Through the process 15.3fold increase in purity with a specific activity of 158.7 U/mg proteins was obtained. The molecular weight of the enzyme determined by SDS-PAGE was found to be 61 kDa. The enzyme was optimally active at pH 5 and 50°C, starch as substrate. This enzyme was almost 60% stable at 600C even after 50 minutes of incubation. It was strongly activated by metal ions such as Mn2+ and Fe2+.

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

Production of plant cell wall degrading enzymes by monoculture and co-culture of Aspergillus niger and Aspergillus terreus under SSF of banana peels

Filamentous fungi are considered to be the most important group of microorganisms for the production of plant cell wall degrading enzymes (CWDE), in solid state fermentations. In this study, two fungal strains Aspergillus niger MS23 and Aspergillus terreus MS105 were screened for plant CWDE such as amylase, pectinase, xylanase and cellulases (β-glucosidase, endoglucanase and filterpaperase) usi...

متن کامل

Partial purification and characterization of α-amylase produced by Aspergillus oryzae using spent-brewing grains

Solid-state fermentation (SSF) was carried out to produce α-amylase from Aspergillus oryzae (IFO 30103) using spent brewing grains (SBG) as substrate. A maximum of 11296 U/gds amylase activity was obtained after 48 h of fermentation. The extracted enzyme was subjected to partial purification by ammonium sulphate fractionation. Maximum specific activity was obtained with 40-70% fraction. SDS-PAG...

متن کامل

Production and Characterization of "-Amylase from Aspergillus niger JGI 24 Isolated in Bangalore

Five fungal isolates were screened for the production of "-amylase using both solid-state and submerged fermentations. The best amylase producer among them, Aspergillus niger JGI 24, was selected for enzyme production by solid-state fermentation (SSF) on wheat bran. Different carbon and nitrogen supplements were used to enhance enzyme production and maximum amount of enzyme was obtained when SS...

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

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

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 2011