Enzymes in Milk Product Manufacture

Penicillium roqueforti and P. camemberti produce very active extracellular lipases, which are the principal lipolytic agents in mold-ripened cheeses. They preferentially hydrolyze the short-chain fatty acids in milk fat. P. roqueforti produces two lipases, one with an alkaline pH optimum and the other most active at pH 6 6.5, with slightly differing fatty acid specificities (Menassa and Lamberet, 1982). P. camemberti secretes a single lipase with optimal activity at pH 9 (Lamberet and Lenoir, 1976). 

Lipase preparations from numerous microorganisms, including those mentioned above, have been used in the synthesis of dairy (buttery or cheesy) flavors from milk fat (Arnold et al., 1975 Kilara, 1985) or to enhance flavor development in ripening cheese (Fox, 1988). These include lipases from Rhizomucor (Mucor) miehei (Moskowitz et al., 1977 Huge-Jensen et al., 1987), Achromobacter lipolyticum (Khan et al., 1967), Aspergillus niger 

Picon et al. (1997) included phospholipase C with encapsulated protei-nases added to milk to stimulate the release of proteinase in Manchego cheese. The phospholipase, acted on the soy lecithin used to form the capsules, accelerated ripening of the cheese. 

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