ENZYMOLOGY OF MILK AND MILK PRODUCTS milk because more than 90% of the lipase is associated with the casein micelles while the triglyceride substrates are in fat globules surrounded, and protected, by the fat globule membrane(MFGM). When the MFGM is damaged, lipolysis occurs rapidly, giving rise to hydrolytic rancidity Lipase was first isolated from skim milk and characterized by Fox and Tarassuk in 1967. The enzyme was optimally active at pH9.2 and 37"C and found to be a serine enzyme(inactivated by organophosphates). A lipo- protein lipase(LPL; activated by lipoprotein co-factors)was demonstrated in milk by Korn in 1962 and was isolated by Egelrud and Olivecrona in 72. LPL is, in fact, the principal indigenous lipase in milk and most recent work has been focused accordingly The molecule has been characterized at he molecular, genetic, enzymatic and physiological levels(see Olivecrona et a,1992) In addition to LPL, human milk contains a bile salts-activated lipase which probably contributes to the metabolism of lipids by breast-fed babies who have limited pancreatic lipase activity. Bovine milk and milks from other dairy animals do not contain this enzyme The lipolytic system in most milks becomes active only when the milk MFGM is damaged by agitation, homogenization or temperature fluctu ations. However, some individual cows produce milk which becomes rancid spontaneously, i.e. without apparent activation. Spontaneous rancidity was considered to be due to a second lipase, termed membrane lipase, which was believed to be associated with the mfgm, but recent evidence suggests that LPL is responsible for spontaneous rancidity following activation by a lipoprotein(co-lipase)from blood serum; normal milk will become sponta neously rancid if blood serum is added, suggesting that'spontaneous milks contain a higher than normal level of blood serum. Dilution of'spontaneous milk with normal milk prevents spontaneous rancidity, which consequently not normally a problem with bulk herd milks; presumably, dilution with normal milk reduces the lipoprotein content of the mixture to below the threshold necessary for lipase adsorption atural variations in the levels of free fatty acids in normal milk and the susceptibility of normal milks to lipolysis may be due to variations in the level of blood serum in milk Significance of lipase. Technologically, lipase is arguably the most signi ficant indigenous enzyme in milk. Although indigenous milk lipase may play a positive role in cheese ripening, undoubtedly the most industrially impor tant aspect of milk lipase is its role in hydrolytic rancidity which renders liquid milk and dair ducts unpalatable and eventually unsaleable Lipolysis in milk has been reviewed extensively(Deeth and Fitz-Gerald, 1995). As discussed in Chapter 3, all milks contain an adequate level of lipase for rapid lipolysis, but become rancid only after the fat globule membrane has been damagedENZYMOLOGY OF MILK AND MILK PRODUCTS 323 milk because more than 90% of the lipase is associated with the casein micelles while the triglyceride substrates are in fat globules surrounded, and protected, by the fat globule membrane (MFGM). When the MFGM is damaged, lipolysis occurs rapidly, giving rise to hydrolytic rancidity. Lipase was first isolated from skim milk and characterized by Fox and Tarassuk in 1967. The enzyme was optimally active at pH 9.2 and 37°C and found to be a serine enzyme (inactivated by organophosphates). A lipo￾protein lipase (LPL; activated by lipoprotein co-factors) was demonstrated in milk by Korn in 1962 and was isolated by Egelrud and Olivecrona in 1972. LPL is, in fact, the principal indigenous lipase in milk and most recent work has been focused accordingly. The molecule has been characterized at the molecular, genetic, enzymatic and physiological levels (see Olivecrona et al., 1992). In addition to LPL, human milk contains a bile salts-activated lipase, which probably contributes to the metabolism of lipids by breast-fed babies who have limited pancreatic lipase activity. Bovine milk and milks from other dairy animals do not contain this enzyme. The lipolytic system in most milks becomes active only when the milk MFGM is damaged by agitation, homogenization or temperature fluctu￾ations. However, some individual cows produce milk which becomes rancid spontaneously, i.e. without apparent activation. Spontaneous rancidity was considered to be due to a second lipase, termed membrane lipase, which was believed to be associated with the MFGM, but recent evidence suggests that LPL is responsible for spontaneous rancidity following activation by a lipoprotein (co-lipase) from blood serum; normal milk will become sponta￾neously rancid if blood serum is added, suggesting that ‘spontaneous milks’ contain a higher than normal level of blood serum. Dilution of ‘spontaneous milk’ with normal milk prevents spontaneous rancidity, which consequently is not normally a problem with bulk herd milks; presumably, dilution with normal milk reduces the lipoprotein content of the mixture to below the threshold necessary for lipase adsorption. Natural variations in the levels of free fatty acids in normal milk and the susceptibility of normal milks to lipolysis may be due to variations in the level of blood serum in milk. Sign8cance of lipase. Technologically, lipase is arguably the most signi￾ficant indigenous enzyme in milk. Although indigenous milk lipase may play a positive role in cheese ripening, undoubtedly the most industrially impor￾tant aspect of milk lipase is its role in hydrolytic rancidity which renders liquid milk and dairy products unpalatable and eventually unsaleable. Lipolysis in milk has been reviewed extensively (Deeth and Fitz-Gerald, 1995). As discussed in Chapter 3, all milks contain an adequate level of lipase for rapid lipolysis, but become rancid only after the fat globule membrane has been damaged