Purification of Bacillus circulans F-2 amylase and its general properties.
نویسندگان
چکیده
منابع مشابه
extraction and acetylation of purified trypsin from bovin pancreas and study of some its physico-chemical properties
آنزیم تریپسین در شرایط قلیایی ناپایدار می باشد .و فعالیت پروتئولیتیکی تریپسین منجربه خود هضمی آن در جایگاههای خاصی می گردد. بنابر این آنزیمی با ناپایداری بالا محسوب میگردد. در سالهای اخیر موفق شدند که با ایجاد تغیرات شیمیایی با اضافه کردن فلزات خاص ، کلسیم و یا عمل استیلاسیون منجر به افزایش پایداری آنزیم تریپسین گردند. مطالعات در حال حاضر نشان می دهد که تریپسین استیله شده فعالیت آنزیمی خود را ...
15 صفحه اولTwo-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 کاملNOTES Partial purification and some properties of α-amylase from Bacillus subtilis KIBGE-HAS
An extracellular α-amylase from Bacillus subtilis KIBGEHAS was partially purified by ultrafiltration and ammonium sulphate precipitation with 19.2-fold purification and specific activity of 4195 U/mg. The enzyme showed relatively high thermostability and retained 62% of its activity when kept at 70°C for 15 min. α -Amylase was highly stable at −18°C and loss of activity was very low during stab...
متن کاملExtraction and Purification of Lactoferrin from Camel Milk and Investigation of Its Amylase Activity
Background and purpose: Lactoferrin is found in mucus, milk, and colostrum secretions and has antimicrobial activities, improves iron absorption, and enhances immune responses. Lactoferrin has the ability to degrade starch. The aim of this study was to investigate the preservation of milk lactoferrin enzymatic activity after purification by ion exchange chromatography. Materials and methods: ...
متن کاملPurification and Biochemical Characterization of Novel Fibrinolytic Protease Produced by Mesophilic Bacillus Circulans Gd25
A novel fibrinolytic protease from Bacillus circulans GD25 was isolated and characterized for the fibrinolytic activity. The fibrinolytic protease was purified by ammonium sulphate fractionation (70%) and subjected to chromatographic methods like Sephadex G-50, DEAE –Sephadex A-50 columns. The purified enzyme has an approximately 38 kDa in size by SDS-PAGE and gel filtration. Optimum activity w...
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ژورنال
عنوان ژورنال: Agricultural and Biological Chemistry
سال: 1983
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.47.511