Production of an extracellular lipase from Candida lipolytica and parameter significance analysis by Plackett‐Burman design

Abstract

AbstractThe enzyme lipase (triacylglycerol hydrolase, EC 3.1.1.3) hydrolyses triacylglycerols to fatty acids, mono‐ and di‐acylglycerols along with a glycerol moiety and are important biocatalysts in industrial applications. In this study, the production of a novel extracellular lipase by Candida lipolytica NRRL‐Y‐1095 using shaking culture was performed. Different chemically enriched fermentation media were evaluated for enzyme activity and one was found to be optimal. Temperature (30°C), initial pH (6) and rate of incubation (48 h) were found complimentary for better enzyme secretion from the yeast cells. The size of inoculum (4 mL, 16 h old) was also optimized. Urea and olive oil at a level of 2 and 1.5 (% w/v) were found to be the best sole nitrogen and carbon sources, respectively. Over 50‐fold enhancement in lipase production (4.01 U) was achieved by the culture when the process parameters including incubation period, sucrose level, initial pH, inoculum size and addition of urea were further identified using the 2‐factorial Plackett–Burman experimental design and response surface methodology. In particular, the addition of 5 g/L sugar under the optimized conditions depicted that the results were highly significant (p≤0.05). Further studies will aim at scale‐up studies in a rotary or drum bioreactor as a pre‐requisite for the commercial exploitation of the batch process.