Castor chemistry is a complex subject and an extensive focus has been made so far over its lipid components and quantitative magnitude of them.However biochemists have realized well the macromolecular co-ordination at the cellular level to cause the emergence of complex traits that is witnessed at the phenotypic level.This logic stood as one of the basis for persuasion of research in castor enzyme chemistry associated with edible oil metabolism.
Scientists of this study have made a crude enzyme extract,soluble at acidic pH and incubated it with multiple, lipid substrates (reactants) purified of castor oil origin.They were able to observe a differential hydrolytic activity over the substrates with lipids having short chain saturated and long chain unsaturated fatty acids being catalytically susceptible to a maximum extent which led the researchers to identify acidic lipases in their extract.They further confirmed that their crude extract is infact a lipase mixture through its biased sensitivity to inhibitors and substrates. Enzyme kinetics data revealed that the enzyme mixture tends to follow a complex order and demand for an external emulsifier to achieve an accelerated catalytic action,proves to be a typical behaviour linked with catabolic lipases.
Experimental research is comprehensive to initiate in-depth enzyme characterization in multiple biochemical dimensions. It followed a classical pattern in biochemistry so far in molecular profiling of seed materials that has not been studied in the concerned direction in past.Purification and in vitro analytical studies in these acidic lipases would answer their significance in lipid turnover processes in castor beans.