EC Number |
General Stability |
Reference |
---|
3.4.22.32 | bromelain immobilized to IDA-Sepharose 6B matrix loaded with Cu2+, Ni2+ and Zn2+ is more resistant to thermal inactivation, as evidenced by retention of over 50% activity after incubation at 60°C |
681487 |
3.4.22.32 | Casein stabilizes against heat inactivation |
30297 |
3.4.22.32 | denaturation in guanidine hydrochloride, the deglycosylated enzyme is more sensitive than the glycosylated one, midpoints of transition are at 2.28 M and 2.86 M, respectively |
650260 |
3.4.22.32 | dextran (D70) and polyethylene glycol (P12 and P20) destablize native bromelain structure |
753856 |
3.4.22.32 | enzymatic activity of bromelain remains uninfluenced by the immobilization of heparin on it |
680253 |
3.4.22.32 | enzyme affinity-bound to a Sepharose matrix precoupled with the lactin concanavalin A is more stable to thermal inactivation than native enzyme or enzyme covalently coupled to the CNBr-activated Sepharose |
664432 |
3.4.22.32 | glutaraldehyde-crosslinked bromelain has comparable activity to the native enzyme, is more stable against urea, guanidine hydrochloride and temperature-induced inactivation and exhibit better storage ability compared to the unmodified protease |
677901 |
3.4.22.32 | glycerol and sorbitol are acting as stabilizers at all concentrations while sucrose and trehalose are destabilizers at lower concentrations, however, act as stabilizers at higher concentrations. Urea and guanidine hydrochloride are denaturants except at lower concentrations |
731938 |
3.4.22.32 | immobilization on amino-Sepharose leads to higher proteolytic activity and remarkably enhanced thermal stability as compared to soluble bromelain and that coupled to CNBr- activated Sepharose |
682719 |
3.4.22.32 | immobilized bromelain shows a higher half-life respect to the free enzyme. The addition of free cysteine during immobilization phase, improves bromelain half-life more than 4folds |
731526 |