| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10541657 | Food Chemistry | 2012 | 9 Pages |
Abstract
⺠Religiosin B is novel milk-clotting serine protease from a vegetal source. ⺠Enzyme is active over a wide range of pH (5.5-11.0) and temperature (20-75 °C). ⺠Enzyme reveals high structural and conformational integrity against denaturants, organic solvents and metal ions. ⺠Enzyme exhibits milk-clotting activity with high MCA/PA of 803.22 ± 23.67 U/OD 660 nm and also works well in alkaline medium. ⺠Enzyme is quite resistant to autodigestion at higher concentration as well as in presence of other additives.
Keywords
TCAPMSFTEMEDPAGEIEFCBBDTNBDEAEFicus religiosaGuHClEGTADTTIAASBTISDSBSACoomassie Brilliant BlueDMSOβ-mercaptoethanolβ-Mebovine serum albuminMilk-clotting enzymeEDTAEthylenediaminetetraacetic acidtrichloroacetic acidiodoacetic acidpolyacrylamide gel electrophoresisdiethylaminoethylDimethyl sulfoxidesodium dodecyl sulphateSerine proteasePhenylmethanesulfonyl fluorideLatexsoybean trypsin inhibitorGuanidine hydrochloride
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Moni Kumari, Anurag Sharma, M.V. Jagannadham,