Purification and properties of phospholipase A1 produced by Corticium centrifugum.
نویسندگان
چکیده
منابع مشابه
Soybean Oil Degumming by Immobilized Phospholipase A1
In the present study, we investigated the ability of an immobilized phospholipase A1 (PLA1) in degumming of soybean oil. The enzyme was immobilized by simple adsorption on bentonite without any further modification. The free and immobilized PLA1 were characterized by Fourier Transform InfraRed (FT-IR) spectroscopy and X-Ray Diffraction (XRD). The immobilizat...
متن کاملPURIFICATION AND PROPERTIES OF AN EXTRACELLULAR PROTEASE PRODUCED BY PENICIUIUM EXPANSUM
Penicilliurn expamum grown in a medium with rice husk as a carbon source produced an extracellular protease. The protease enzyme was isolated from culture broth by fractionation with acetone and column chromatography on Sephadex G- 100 and DEAE A-50. The protease enzyme was purified about 17.47 fold, with a recovery of 14%. The purified protease was homogenous on SDS polyacrylarnide disc ge...
متن کاملPurification and properties of a membrane-bound phospholipase A1 from Mycobacterium phlei.
A phospholipase A1 bound tightly to the membranes of Mycobacterium phlei cells was purified approximately 500fold to near homogeneity by extraction with Triton X-100, delipidation with organic solvents, solubilization with sodium dodecyl sulfate, column chromatographies on Sephadex G-200 in the presence of sodium dodecyl sulfate and on DEAE-cellulose in the presence of BRIJ 58, and sodium dodec...
متن کاملcontrol of the optical properties of nanoparticles by laser fields
در این پایان نامه، درهمتنیدگی بین یک سیستم نقطه کوانتومی دوگانه(مولکول نقطه کوانتومی) و میدان مورد مطالعه قرار گرفته است. از آنتروپی ون نیومن به عنوان ابزاری برای بررسی درهمتنیدگی بین اتم و میدان استفاده شده و تاثیر پارامترهای مختلف، نظیر تونل زنی(که توسط تغییر ولتاژ ایجاد می شود)، شدت میدان و نسبت دو گسیل خودبخودی بر رفتار درجه درهمتنیدگی سیستم بررسی شده اشت.با تغییر هر یک از این پارامترها، در...
15 صفحه اولPurification and properties of lysozyme produced by Staphylococcus aureus.
A method based on cold ethyl alcohol fractionation at different pH levels and ionic strengths and on gel filtration on a Sephadex G-200 column was used to concentrate and purify lysozyme from the culture supernatant fluid of Staphylococcus aureus strain 524. The final, nondialyzable product exhibited a 163-fold rise in specific activity over that of the starting material. Staphylococcal lysozym...
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: Agricultural and Biological Chemistry
سال: 1979
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.43.517