EFFECT OF CULTURAL AND ASSAY CONDITIONS OF CELL. BOUND LIPASE FROM A BACTERIAL ISOLATE SJ-15REENA GUPTA, JYOTI SAROOP AND SHALINI JAINAbstract Isolate SJ-15, which exhibited cell-bound lipase activity was isolated from the waste of an oil extraction plant. The cell bound lipase was 84.2% solubilized by SDS (0.1%). Production of the enzyme was substantially enhanced when the carbon and nitrogen sources and initial pH of the culture medium were consecutively optimized. Soyabean oil (1% w/v) and urea (0.3% w/v) were found to be the best carbon and nitrogen source respectively; giving high enzyme production (230U/g) when initial culture pH was 6.5 The kinetic characteristics of the enzyme indicated the highest activity at 50°C and pH 8.5 (290 U/g). The enzyme activity was mildly enhanced by metal ions Cu2+, Li + and strongly inhibited by Zn2+ ions.
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