مقاله انگلیسی لیپازهای میکروبی: بیوکاتالیست های مفید برای صنایع غذایی
Abstract
Graphical abstract
Keywords
Introduction
Application of microbial lipases in food industry
Future directions
Conclusions
Declaration of competing interests
Author contributions
Acknowledgments
References
ABSTRACT
Lipases (triacylglycerol acylhydrolases, EC 3.1.1.3) are one of the largest groups of enzymes and are used in various industrial processes. Lipases of microbial origin are currently receiving increased attention for industrial application as microorganisms grow quickly and are easily genetically manipulated. Furthermore, they offer several advantages, such as catalysis of diverse reactions, high specificity, high yields, low energy consumption and reduced processing time and production costs. There is a relentless ongoing effort to optimise the production of microbial lipases for potential application in the food industry. In this context, this review highlights the most promising techniques for producing microbial lipases and the recent applications of these lipases in dairy, oils and fats, bakery and confectionery, meat, flavours and aromas and other food industries. Microbial lipases are normally obtained by fermentation, but the high costs of carbon and nitrogen sources limit the process. To overcome this problem, low-cost agro-industrial residues in the lipase production process are explored. To obtain lipases with high yields and improved characteristics, the technique of protein engineering is described as promising, and the immobilization method that allows the recycling of lipases to improve their catalytic performance is focused. Due to their catalytic properties and versatility, lipases of microbial origin are considered extremely important catalysts in the food industry, meeting the demand for tastier foods with pleasant aromas and textures. Therefore, microbial lipases are considered safe and sustainable biocatalysts.
Introduction
Lipases as biocatalysts Lipases are recognized as lipolytic enzymes belonging to the serine hydrolase group, responsible for catalysing the hydrolysis of estercarboxylic bonds of triacylglycerols (TAG) with the release of free fatty acids, diglycerides (DAG), monoglycerides (MAG) and glycerol (Chen et al., 2003; Jaeger et al., 1994; Nagarajan, 2012). Lipases preferentially hydrolyse substrates with long-chain fatty acids greater than 10 carbons. However, lipases can also hydrolyse substrates with shortand intermediate-chain fatty acids (Anthonsen et al., 1995; Chen et al., 2003; Jaeger et al., 1999). In addition to hydrolysis, in which the nucleophilic agent is a water molecule, lipases can catalyse the reverse reaction, esterification (Borrelli & Trono, 2015). Depending on the transformation of the ester group, other reactions can also be catalysed, such as (1) transesterification, which encompasses reactions with alcohols acting as nucleophiles, for example, glycerolysis; (2) interesterification, which is characterized by exchange between the substituents of two different esters and (3) acidolysis and (4) aminolysis, which, as the names suggest, refer to breakdown by carboxylates and amines as nucleophilic agents, respectively (Alfonso & Gotor, 2004; Farf´ an et al., 2013; Otera, 1993; Parker & Baker, 1968) (Fig. 1). Due to the versatility of reactions catalysed by lipases, they are considered biotechnologically important biocatalysts, becoming green alternatives to chemical methods, providing safe and invaluable tools for industrial transformations to synthesize natural or synthetic materials with lower energy consumption under moderate reaction conditions (Memarpoor-Yazdi et al., 2017)