Abstract
In this study, extreme halophilic archean Natrialba asiatica was utilized as a new source for lipase production. Lipases from halophilic archaea are appealing for utilization in assorted industrial and biotechnological applications. The optimum temperature and pH of N. asiatica lipase in the crude mixture were 50 °C and 10, respectively. The growth conditions influencing lipase production were determined using a two-level fractional factorial Plackett–Burman design. Among the 9 factors screened, MgCl2 concentration, temperature, and shaking were found to be effective. The optimum levels of these factors for the production process were determined by employing the central composite design of response surface methodology. The 27 g L-1 of MgCl2, 50 °C, and 133 rpm were determined as optimized conditions for lipase production. The enzyme activity increased from 3.39 to 6.1 U mL-1 using predicted optimum levels. These findings help understanding factors affecting the production of lipase by halo-archean N. asiatica. Moreover, using the optimized level of temperature, shaking, and MgCl2, it is possible to increase the production of valuable alkaline lipase by N. asiatica.
Highlights
IntroductionLipases (triacylglycerol acyl-hydrolases, E.C. 3.1.1.3) catalyze the hydrolase reaction of triacylglycerol into fatty acids and glycerol
Lipases catalyze the hydrolase reaction of triacylglycerol into fatty acids and glycerol
This means that olive oil, lactose, and peptone used in the culture of N. asiatica as carbon and nitrogen sources have not effect on lipase production and could be replaced by other components
Summary
Lipases (triacylglycerol acyl-hydrolases, E.C. 3.1.1.3) catalyze the hydrolase reaction of triacylglycerol into fatty acids and glycerol. They usually exhibit good chemoselectivity, regioselectivity, and enantioselectivity besides broad substrate specificity (Joseph et al, 2008) These broad specifications made lipases one of the powerful essentials in several biotechnological aspects including synthesis of biopolymer, biodiesel, pharmaceuticals, agro-chemicals, and flavor compounds (Jaeger & Eggert, 2002). The proteins of these organisms can remain active in high salt concentrations (Karan et al, 2012) These adaptations besides the existing robust nature of lipases make halophilic lipases especially attractive for industrial and biotechnological applications. Some of the factors influencing the optimal growth of a microorganism do not play a role in lipase production but in some cases have a negative effect. The lipase production process was optimized using a model that had been introduced by RSM to gain higher lipase production and was compared with unoptimized process
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