PURIFICATION, CHARACTERIZATION AND SEQUENCING OF AMYLASE A FROM ALKALIPHLIC BACILLUS LICHENIFORMIS STRAIN-MK7
نویسندگان
چکیده
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 کاملtwo-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 کاملCharacterization of an a-Amylase with Broad Temperature Activity from an Acid-Neutralizing Bacillus cereus Strain
Bacillus sp. GUF8, isolated from acidic soil samples of a tea farm was identified as Bacillus cereus, based on 16S rDNA sequencing and standard bacterial identification methods. Following optimization of enzyme production, the resulting α-amylase was purified by acetone precipitation and ion exchange chromatography. Consequently, thermostability and kinetic parameters of the purified enzyme wer...
متن کاملSingle 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 کاملPurification 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 کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Research Journal of Applied Biotechnology
سال: 2016
ISSN: 2356-9433
DOI: 10.21608/rjab.2016.59670