Purification and Characterization of Milk Clotting Enzyme Produced by Rhizomucor Rmiehei
نویسندگان
چکیده مقاله:
Milk clotting enzyme (M CE) produced by: Rhizomucor miehei was purified and characterized.The enzyme was purified 220.29-fold with specific activity about 14444.2 U/mg protein byultrafiltration, ammonium sulfate fractionation, Sephacryl S-300 chromatography. The maximumenzyme activity was at 65°C.The milk clotting activity was decreased steadily as pH is increased and indicated maximumactivity at pH 5.3.Ferthermore we did some computational methods for understanding the changesin energy.
منابع مشابه
purification and characterization of milk clotting enzyme produced by rhizomucor rmiehei
milk clotting enzyme (m ce) produced by: rhizomucor miehei was purified and characterized.the enzyme was purified 220.29-fold with specific activity about 14444.2 u/mg protein byultrafiltration, ammonium sulfate fractionation, sephacryl s-300 chromatography. the maximumenzyme activity was at 65°c.the milk clotting activity was decreased steadily as ph is increased and indicated maximumactivity ...
متن کاملExtraction of milk-clotting enzyme produced by solid state fermentation of Aspergillus oryzae.
Studies on the extraction of milk-clotting enzyme after solid-state fermentation (SSF) of wheat bran by a local strain of Aspergillus oryzae LS1 were done. The extraction of the enzyme was found to be depended on different parameters like nature of extractant, soaking time, temperature etc. From different inorganic and organic extractants, calcium chloride (0.05%) and glycerol (40%) were found ...
متن کاملAffinity Purification and Characterization of Recombinant Bacillus sphaericus Phenylalanine Dehydrogenase Produced by pET Expression Vector System
Cloning and expression of the L-phenylalanine dehydrogenase gene, from B. sphaericus in E. coli were done. The gene was cloned in the vector pET16b and transformed into E. coli BL21 (DE3). The functional form of the L-phenylalanine dehydrogenase enzyme was purified by affinity purification techniques, taking advantage of the ability of this enzyme to bind to the nucleotide site affinity dye, Re...
متن کاملPurification and characterization of an enzyme produced by Treponema denticola capable of hydrolyzing synthetic trypsin substrates.
An enzyme from Treponema denticola that hydrolyzes a synthetic trypsin substrate, N-alpha-benzoyl-L-arginine-p-nitroanilide (BAPNA), was purified to near homogeneity, as judged by gel electrophoresis. The molecular weight of the enzyme was estimated to be ca. 69,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and ca. 50,000 by gel filtration on Sephadex G-100. The pH optimum fo...
متن کاملCharacterization of partially purified milk‐clotting enzyme from sunflower (Helianthus annuus) seeds
This study was aimed to extract milk-clotting enzyme from sunflower seeds and to determine its potentiality for manufacturing white soft cheese from cows and goats milk. The seeds were blended and extracted using two types of buffers and milk-clotting and proteolytic activities were evaluated. The enzyme was partially purified using ammonium sulfate fractionation techniques. Results indicated t...
متن کاملPurification and biochemical characterization of polygalacturonases produced by Aureobasidium pullulans.
The extracellular polygalacturonases produced by Aureobasidium pullulans isolated from waters of the Danube river were partially purified and characterized. The pH optima of polygalacturonases produced in the first phases of cultivation (48 h) and after 10 d as well as their optima of temperature, thermal stabilities, molecular masses, isoelectric points, action pattern and ability to cleave po...
متن کاملمنابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ذخیره در منابع من قبلا به منابع من ذحیره شده{@ msg_add @}
عنوان ژورنال
دوره 5 شماره 3
صفحات 29- 34
تاریخ انتشار 2008-11-01
با دنبال کردن یک ژورنال هنگامی که شماره جدید این ژورنال منتشر می شود به شما از طریق ایمیل اطلاع داده می شود.
میزبانی شده توسط پلتفرم ابری doprax.com
copyright © 2015-2023