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STUDIES ON THE INACTIVATION OF LYSOZYME BY MALONALDEHYDE
Author(s) -
CHANDER RAMESH,
SHEREKAR S. V.,
GORE M. S.
Publication year - 1981
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1981.tb00681.x
Subject(s) - lysozyme , incubation , chemistry , enzyme , lytic cycle , context (archaeology) , size exclusion chromatography , chromatography , degradation (telecommunications) , enzyme assay , filtration (mathematics) , biochemistry , biology , immunology , paleontology , telecommunications , virus , computer science , statistics , mathematics
The interaction of malonaldehyde with lysozyme has been assessed with reference to incubation time, pH, concentration and aging. Gel filtration studies revealed that freshly prepared malonaldehyde contains a small proportion of compounds absorbing at 267 and 350 nm, which shows significant increase upon incubation of malonaldehyde. While higher concentration of malonaldehyde leads to inactivation of enzyme, lower concentration (2.5 mM) stimulates the lytic function of lysozyme. Stimulation and inactivation of the enzyme have been discussed in the context of degradation of malonaldehyde.