Abstract
Recently, the application of lipase enzyme as biocatalyst in the conversion of waste cooking oil (WCO) to free fatty acids and glycerol has been trending well. Therefore, the present study attempts to use WCO which is found in abundance in Malaysia as the substrate for halal microbial lipase conversion to glycerol which can be exploited in the food industry. The workability of free lipase for WCO conversion, however suffers severely due to potential denaturation of the enzyme and extended reaction time. Thus, this study embraced the immobilization method to encapsulate crude lipase extracted from Rhodococcus pyridinivorans strain UCC 0009 in gellan gum and calcium alginate, respectively and compared their ability for WCO conversion to free crude lipase. The gellan gum and calcium alginate-immobilized crude lipase evidently exhibited greater WCO conversion, demonstrating 2.18-fold and 1.61-fold enhanced lipase activity, respectively in comparison to free crude lipase. The repeated reuse of the gellan gum-immobilized crude lipase maintained reasonable lipase activity for 9 cycles, retaining an average 85 % WCO conversion for the first seven cycles and 67 % conversion in the subsequent batches. Thus, the immobilized halal lipase can be foreseen as a green substitute to chemical catalyst for WCO conversion which meets the worldwide demand for clean technologies.
Highlights
Many industries namely textiles, medicines, leather, food and detergents have extensively accommodated the use of enzymes in their practices since the emergence of enzymology [1]
This study embraced the immobilization method to encapsulate crude lipase extracted from Rhodococcus pyridinivorans strain UCC 0009 in gellan gum and calcium alginate, respectively and compared their ability for waste cooking oil (WCO) conversion to free crude lipase
The present study revealed that the utilization of crude lipase extracted from Rhodococcus pyridinivorans strain UCC 0009 and immobilized in gellan gum yielded in greater WCO conversion in contrast to calcium alginate-immobilized crude lipase and free crude lipase, respectively which may be possibly due to enhanced enzyme-substrate interaction
Summary
Medicines, leather, food and detergents have extensively accommodated the use of enzymes in their practices since the emergence of enzymology [1]. The broad biochemical diversity of microorganisms and the achievability of large-scale production are the main factors that turn microorganisms into the most commonly used source for the production of industrial enzymes [1]. Industrially important enzyme that can be produced economically from microorganisms and used as a biocatalyst in a variety of industrial applications, including food processing technology, oil processing, medicine and biodegradation [4]. Microbial lipase is important because it is easy to ferment and purify and presents itself as one of the most common sources for biodiesel production through transesterification [4]. Lipase immobilisation on suitable support is the key parameter to achieve enhanced stability, reusability, easy product separation and recovery, reduced cost for lipase production and improved control of reactions [6]
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