| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 10539967 | Food Chemistry | 2012 | 9 Pages |
Abstract
⺠Neriifolin S is a dimeric serine protease with broad substrate specificity. ⺠Enzyme is active over a wide range of pH (6-10.5) and temperature (20-60 °C). ⺠Enzyme reveals high conformational stability against chaotrops and organic solvents. ⺠Enzyme exhibit milk clotting activity with higher MCA/PA of 433.25 U/OD 660 nm. ⺠Enzyme is resistant to autodigestion at higher concentration.
Keywords
DTNBEuphorbia neriifoliaGuHClEuphorbiaceaediisopropylfluorophosphatePMSFSBTIPAGECBBDFPGuSCNEGTATCAβMEDTTSDSMALDI-TOFIAA5,5′-dithiobis-(2-nitrobenzoic acid)BSACoomassie Brilliant BlueDMSOβ-mercaptoethanolbovine serum albuminEDTAtrichloroacetic acidpolyacrylamide gel electrophoresisTris–HCldimethylsulphoxideDimericdithiothreitolsodium dodecyl sulphateSerine proteasephenylmethanesulphonyl fluorideguanidine thiocyanateGuanidine hydrochloride
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Ravi Prakash Yadav, Ashok Kumar Patel, M.V. Jagannadham,