Lipases for the Production of Food Components

Abstract

One of the first attempts to summarize the then current knowledge of the industrial application of enzymes was made by Godfrey and Reichelt in 1983. 1 This book contained contributions from industrial, academic and government writers and was widely recognized as a major contribution to disseminating enzyme knowledge. Comprehensive though this volume was, the amount of space allocated to lipases was one of the smallest and only one lipase from calf stomach was listed in the appendix of enzyme types. At that time, the main recognized application was in the dairy industry for the accelerated ripening of cheese and production of high-intensity cheese flavours.However, within a very short time frame the number of actual and potential lipase applications had increased vastly and within 10 years it had grown to include both food-related and technical applications. The reason for this explosion in applications can be seen to be a result of a number of different discoveries in enzyme biochemistry, linked with new production technologies and significant research resources being applied by the lipase producing and using companies.The first enzyme applications were in the field of flavour generation and used the hydrolytic action of the lipase to generate free fatty acids that increased the 'cheesy' flavour of milk products. Short chain fatty acids from milk liberated by starter culture lipases were known to be involved in the natural ripening of some cheese types and the cheese makers tried to mimic this process. However, this application was limited in potential due to the relatively small amount produced of this cheese type. In 1984, however, Zaks and Klibanov 2 demonstrated that enzymes could function in micro aqueous environments, indicating the possibility that lipases could function in non-aqueous systems. Synthesis reactions, in which hydrolysis is reversed, became possible and opened up a new research area into lipase function.Within this sector, one of the first products were specific fats (cocoa butter equivalents) as described by Coleman and Macrae 3 and Matsuo et al. 4 They utilized an immobilized lipase to exchange fatty acids on a triglyceride with the desired ones, to produce a cocoa butter-like fat. Macrae 5 describes the use of a lipase product absorbed onto a kieselguhr matrix to convert a mixture of palm mid fraction and stearic acid into a cocoa butter equivalent (CBE)-like product containing increased levels of the desired triglycerides, 1(3)-palmityl-3(1)-stearyl-2-monooleine (POSt) and 1,3-distearyl-2-monooleine (StOSt). The immobilized lipase was prepared by making a slurry of the enzyme with kieselguhr and then adding a solvent such as acetone or an alcohol (ethanol or methanol) to precipitate the enzyme onto the inorganic Enz y mes in Food Technology , Second edition Edited by Robert J. Whitehurst and Maarten van Oort

Industrial use of immobilized enzymes

“…The commercialization of this process was enabled by the production of a robust enzyme particle (Novozymes Lipozyme s TL IM) containing a cost-effective lipase. 207,209,222 Archer Daniels Midland commercialized EIE-based production of trans-free margarines and shortenings using Lipozyme s TL IM in July 2002. 207,209 To address the gradual loss of enzyme activity in a single fixed bed reactor when operated continuously for commercial production, several reactors were operated in series.…”

Structure–energy relationship of food materials using differential scanning calorimetry

“…The main function of lipase enzyme is to hydrolyze triglyceride molecules into glycerol, fatty acid, mono‐, and diacylglycerols. Another group of enzymes named as esterases are characterized by cleaving the carboxylic ester bonds (Cowan, 2010). For instance, enzymes that attack substrates with an acyl chain length greater than 10 carbon atoms are categorized as lipases, whereas those containing less than 10 carbon atoms are classified under family of esterases (Gunstone, 2004).…”

Moving towards a Competitive Fully Enzymatic Biodiesel Process

“…Moreover, it requires a strong chelating agent such as citric acid at higher concentrations (0.1%) to achieve a suitable phosphorus reduction. Such conditions can hardly be reached with milder citric acid concentrations or even with phosphoric acid [83], thus making it difficult to reach the required phosphorus content in the final biodiesel.…”