Journal of Dairy Science and Biotechnology

Korean Society of Dairy Science and Biotechnology (한국낙농식품응용생물학회)
권호 표지
DOI QR코드

DOI QR Code

Effects of Heat Treatment on the Nutritional Quality of Milk: V. The Effect of Heat Treatment on Milk Enzymes

우유의 열처리가 우유품질과 영양가에 미치는 영향: V. 열처리가 우유효소에 미치는 영향

  • Shin, Hanseob (Division of Animal Science, Chonnam National University) ;
  • Oh, Sejong (Division of Animal Science, Chonnam National University)
  • 신한섭 (전남대학교 농업생명과학대학 동물자원학부) ;
  • 오세종 (전남대학교 농업생명과학대학 동물자원학부)
  • Received : 2018.03.25
  • Accepted : 2018.03.29
  • Published : 2018.03.31
Download PDF
⟨ Previous Next ⟩

Abstract

Heat treatment is the most popular processing technique in the dairy industry. Its main purpose is to destroy the pathogenic and spoilage bacteria in order to ensure that the milk is safe throughout its shelf life. The protease and lipase that are present in raw milk might reduce the quality of milk. Plasmin and protease, which are produced by psychrotrophic bacteria, are recognized as the main causes of the deterioration in milk flavor and taste during storage. The enzymes in raw milk can be inactivated by heat treatment. However, the temperature of inactivation varies according to the type of enzyme. For example, some Pseudomonas spp. produce heat-resistant proteolytic and lipolytic enzymes that may not be fully inactivated by the low temperature and long time (LTLT) treatment. These types of enzymes are inhibited only by the high temperature and short time (HTST) or ultra-high temperature (UHT) treatment of milk.

Keywords

References

  1. Adams Jr., D. M., Barach, J. T. and Speck, M. L. 1979. Inactivation of heat resistant bacterial proteases in UHT treated milk. U.S. Patent, Nov. 20, 4, 175, 141.
  2. Adams, D. M., Barach, J. T. and Speck, M. L. 1975. Heat resistant proteases produced in milk by psychotrophic bacteria of dairy origin. J. Dairy Sci. 58:828-835. https://doi.org/10.3168/jds.S0022-0302(75)84645-5
  3. Adams, D. M., Barach, J. T. and Speck, M. L. 1976. Effect of psychotrophic bacteria from raw milk on milk proteins and ability of milk proteins to ultrahigh temperature treatment. J. Dairy Sci. 59:823-827. https://doi.org/10.3168/jds.S0022-0302(76)84282-8
  4. Aimutis, W. R. and Eigel, W. N. 1982. Identification of ${\gamma}$-casein as plasmin-derived fragments of bovine ${\alpha}_{s1}$-casein. J. Dairy Res. 65:175-181. https://doi.org/10.3168/jds.S0022-0302(82)82173-5
  5. Alais, c. and Ged, J. 1978. Effects of sterilization by friction on the milk enzymes. Int. Dairy Congr. E:612.
  6. Anderson, R. E., Hedlund, C. B. and Jonsson, U. 1979. Thermal inactivation of a heat resistant lipase produced by the psychotrophic bacterium Pseudonanas fluorescens. J. Dairy Sci. 62:361-367. https://doi.org/10.3168/jds.S0022-0302(79)83252-X
  7. Anderson, M. 1983. Milk lipase and off-flavour development. J. Soc. Dairy Technol. 36:3-7. https://doi.org/10.1111/j.1471-0307.1983.tb02520.x
  8. Andrews, A. 1975. Properties of aseptically packed ultra high-temperature milk, 111. Formation of polymerized proteins during storage at various temperatures. J. Dairy Sci. 42:89-99.
  9. Andrews, A. T. 1983. Proteinases in normal bovine milk and their action on caseins. J. Dairy Sci. 50:45-55.
  10. Andrews, A. T. and Pallavicini, C. 1973. Bovine milk acid phosphatase. I. Some kinetics studies and other properties using a partially purified preparation. Biochim, Biophys. Acta. 321:197-209. https://doi.org/10.1016/0005-2744(73)90074-0
  11. Andrews, A. T. and A1ichanidis, E. 1983. Proteolysis of caseins and the proteosepeptone fraction of bovine milk. J. Dairy Res. 50:275-290. https://doi.org/10.1017/S0022029900023116
  12. Astrup, T. and Sterndorff, I. 1953. A fibrinolytic system in human milk. Proc. Soc. Exp. Biol. Med. 84:605-609. https://doi.org/10.3181/00379727-84-20727
  13. Aurand, L. W., Boone, N. H. and Giddings, G. G. 1977. Superoxide and singlet oxygen in milk lipid peroxidation. J. Dairy Sci. 60:363-369. https://doi.org/10.3168/jds.S0022-0302(77)83874-5
  14. Ball, E. G. 1939. Xanthine oxidase: Purification and properties. J. Biol. Chem. 128:51-67.
  15. Bandyopadhyay, A. K., Janeja, H. K. and Ganguli, N. C. 1979. Extent of inactivation of xanthine oxidase in milk during processing and gastric digestion. Lebensmittel Wissenschaft und Technologie. 12(1):19-22.
  16. Barach, J. T., Adams, D. M. and Speck, M. L. 1976. Low temperature inactivation in milk of heat-resistant protease from psychotrophic bacteria. J. Dairy Sci. 59:391-395. https://doi.org/10.3168/jds.S0022-0302(76)84218-X
  17. Barach, J. T., Adams, D. M. and Speck, M. L. 1978. Mechanism of low temperature inactivation of a heat resistant bacterial protease in milk. J. Dairy Sci. 61:523-528. https://doi.org/10.3168/jds.S0022-0302(78)94405-3
  18. Bassette, R., Fung, D. Y. C. and Mantha, V. R. 1986. Off- flavors in milk. CRC Critical Review in Food Sci. Nutr. 24(1):1-52. https://doi.org/10.1080/10408398609527439
  19. Baumrucker, C. R. 1980. Purification and identification of ${\gamma}$-glutamyl transpeptidase of milk membranes. J. Dairy Sci. 63: 49-54. https://doi.org/10.3168/jds.S0022-0302(80)82886-4
  20. Bengtsson, G. and Olivecrona, T. 1980. Lipoprotein lipase: Some effects of activator proteins. Eur. J. Biochem. 106:549-555. https://doi.org/10.1111/j.1432-1033.1980.tb04602.x
  21. Bhadsalve, C. H., Shehata, T. E. and Collins, E. B. 1972. Isolation and identification of psychophilic species of Clostridium from milk. Appl. Microbiol. 24:699-706.
  22. Brinham, E. W., Jasewicz, L. and Eittle, C. A. 1961. Acid phosphatase in cream and in skimmilk. J. Dairy Sci. 44:1247-1256. https://doi.org/10.3168/jds.S0022-0302(61)89875-5
  23. Birch, G. G., Bakebrough, N. and Parker, K. J. 1981. Enzymes and food processing. Applied Science Publisher, New York.
  24. Biryukova, Z. A., Selvenznev, V. 1., Dombrovskaya, E. 1. and Makarova, A. 1. 1975. Changes in sterile milk during storage. Food Sci. Technol. Abstr. 6:163.
  25. Bjorck, L. and Claesson, C. 1979. Xanthine oxidase as a source of hydrogen peroxide for the lactoperoxidase system in milk. J. Dairy Sci. 62:1211-1215. https://doi.org/10.3168/jds.S0022-0302(79)83402-5
  26. Bruder, G., Heid, H., Jarasch, E. D., Keenan, T. W. and Mather, 1. H. 1982. Characteristics of membrane-bound and soluble forms of xanthine oxidase from milk and endothelial cells of capillaries. Biochim, Biophys. Acta. 701:357-369. https://doi.org/10.1016/0167-4838(82)90239-4
  27. Bucky, A. R. and Hayes, P. R. 1987. A modified ultra high temperature treatment for reducing microbiol lipolysis in stored milk. J. Dairy Res. 54:275-282. https://doi.org/10.1017/S0022029900025413
  28. Cerbulis, J. and Farrell, H. M. 1977. Xanthine oxidase activity in dairy products. J. Dairy Sci. 60:170-176. https://doi.org/10.3168/jds.S0022-0302(77)83850-2
  29. Christen, G. L. and Marshall, R. T. 1984. Thermostability of lipase and protease of Pseudomanas fluorescens 27 produced in various broths. J. Dairy Sci. 67:1688-1693. https://doi.org/10.3168/jds.S0022-0302(84)81493-9
  30. Christen, G. L., Wang, W. c. and Ren, T. J. 1986. Comparison of the heat resistance of bacterial lipase and protease and the effect on ultra-high temperature milk quality. J. Dairy Sci. 69:2769-2778. https://doi.org/10.3168/jds.S0022-0302(86)80728-7
  31. Christophersen, J. 1980. Uber den einfluB them scher behand lung auf proteasen in lebensmittein. Zeitschrift fur Lebensmattel Technologie und Verfahrenstechnik. 3(2):43-46.
  32. Clare, D. A., Blackstone, B. A. Swaisgood, H. E. and Horton. H. R. 1981. Sulfhydryl oxidase-catalyzed conversion of xanthine dehydrogenase to xanthine oxidase. Arch. Biochem. Biophys. 211:44-47. https://doi.org/10.1016/0003-9861(81)90427-6
  33. Cousin, M. A. 1982. Presence and activity of psychrotrophic microorganisms in milk and dairy prodcts: a review. J. Food Protec. 45:172-207. https://doi.org/10.4315/0362-028X-45.2.172
  34. Cousin, M. A. and Marth, E. H. 1977. Psychotrophic bacteria cause changes in stability of milk to coagulation by rennet or heat. J. Dairy Sci. 60:1042-1047. https://doi.org/10.3168/jds.S0022-0302(77)83986-6
  35. De Konig, P. J., Kaper, J., Rollema, H. S. and Driessen, F. M. 1985. Age thinning and gelation in unconcentrated and concentrated UHT-sterilized skimmilk. Effect of native milk protease. Neth. Milk Dairy J. 39:71-85.
  36. Deeth, H. C. 1983. Homogenized milk and atherosclerotic disease: a review. J. Dairy Sci. 66:1419-1435. https://doi.org/10.3168/jds.S0022-0302(83)81956-0
  37. Deeth, H. C. and Fitzgerald, C. H. 1976. Lipolysis in dairy products: a review. Aust. J. Dairy Technol. 31:53-64.
  38. De Rhan, O. and Andrews, A. T. 1982. The roles of native milk proteinase and its zymogen during proteolysis in normal bovine milk. J. Dairy Res. 49:577-585. https://doi.org/10.1017/S002202990002272X
  39. Diermayr, P., Kroll, S. and Klostermeyer, H. 1987. Mechanisms of heat inactivation of a proteinase from Pseudomonas fluorescens biotype. I. J. Dairy Res. 54:51-60. https://doi.org/10.1017/S002202990002519X
  40. Downey, W. K. 1980. Review of the progress of the dairy science: flavor impairment from pre-and post manufacture lipolysis in milk and dairy products. J. Dairy Res. 47:237-252. https://doi.org/10.1017/S0022029900021117
  41. Driessen, F. M. 1976. Eivitafbraak in stromend gesteriliscerde me1k en melk produkten. Zuivelzicht. 68(22):1314-1515.
  42. Driessen, F. M. 1981. Enzymatische eivitafbraak in Kort/hoog gesteriliseerde melk produkten. I. Produkte van proteinasen door bacterien tijdens hun groei in melk. Voedingsmiddle-lentechnologie 23 Juli, Jaargang 14, nr 15:18-20.
  43. Driessen, F. M. and Van Der Waals, C. B. 1978. Inactivation of native milk protenase by heat treatment. Neth. Milk. Dairy J. 32:245-254.
  44. Driessen, F. M. and Stadhouders, J. 1971. Heat stability of lipase of Alcaligenes viscolactis 23 al, Neth. Milk Dairy J. 25:141-144.
  45. Driessen, F. M. and Stadhouders, J. 1974. Thermal activation and inactivation of exocellular lipa ses of some gram negative bacteria common on milk. Neth. Milk Dairy J. 28:10-14.
  46. Driessen, F, M., and Stadhouders, J. 1978. Enzymatisch bederf in gepasteuriseerde en gesteriliseerde me1k en zuivelprodukten. I. Eivitafbraak. Zuivelzich. 70(44):994-996.
  47. Ebner, K. E. and Schanbacher, F. L. 1974. A comprehensive treatise. In lactation. Vol. 11, Larson, B. L. and V. R. Smith ed, Academic Press.
  48. Egelud, T. and Olivecrona, T. 1972. The purification of a lipoprotein lipase from bovine skim milk. J. Biol. Chem. 247:6212-6217.
  49. Eigel, W. N. 1977. Effect of bovine plasmin on ${\alpha}_{s1}$-B and ${\kappa}$-A casein. J. Dairy Sci. 60:1399-1403. https://doi.org/10.3168/jds.S0022-0302(77)84043-5
  50. Eikakis, J. P. and Woosters, S. C. 1980. Activity of xanthine oxidase in dairy products. J. Dairy Sci. 63:893-904. https://doi.org/10.3168/jds.S0022-0302(80)83023-2
  51. Eitenmiller, R. R. Friend, B. A. and Shahani, K. H. 1971. Comparison of bovine and human milk lysozymes. J. Dairy Sci. 54:762.
  52. Eriksson, C. E. 1969. Nonensymatic lipid oxidation by lacto-peroxidase. Effect of heat treatment. J. Dairy Sci. 53:1649-1653.
  53. Forster, F. L., Montgomery, M. N. and Montoure, J. E. 1961. Some factors influencing the activity of the A-, B-, and C- esterases of bovine milk. J. Dairy Sci. 44:1420-1430. https://doi.org/10.3168/jds.S0022-0302(61)89903-7
  54. Fox, P. F. and Stepaniak, L. 1983. Isolation and some properties of extra-cellular heat-stable lipases from Pseudomonas fluorescens AFT36. J. Dairy Res. 50:77-89. https://doi.org/10.1017/S0022029900032544
  55. Gould, B. S. 1932. The detection of inefficiently pasteurized milk based on a modification of the new Rothen-Fusser test. J. Dairy Sci. 15:230-241. https://doi.org/10.3168/jds.S0022-0302(32)93408-0
  56. Griffiths, H. M., Phillips, J. D. and Muir, D. D. 1981. Thermo- stability of protease and lipase from a number of species of psychotrophic bacteria of dairy origin. J. Appl. Bacterol. 50:289-303. https://doi.org/10.1111/j.1365-2672.1981.tb00894.x
  57. Griffiths, M. M., Phillips, J. D. and Muir, D. D. 1984. Methods for rapid detection of post-pasteurization contamination in cream. J. Soc. Dairy Tech. 37:22-26. https://doi.org/10.1111/j.1471-0307.1984.tb02277.x
  58. Groves, M. L. 1971. Minor milk proteins and enzymes. In milk proteins, Vol. II, Mckenzie, M. A. ed, Academic press, New York.
  59. Grufferty, M. B. and Fox, P. F. 1986. Potassium indate induced proteolysis in ultra he treated milk cluring storage: the role of ${\beta}$-lactoglobulin and plasmin. I. Dairy Res. 53:601-613. https://doi.org/10.1017/S0022029900033124
  60. Guamis, B., Huerta, T. and Garay, E. 1987. Heat inactivation of bacterial proteases in milk before UHT-treatment. Michi-Wissenschaft. 42(10):651-653.
  61. Hansen, A. P. 1985. The effect of different UHT processing pa-rameters on the chemical and physical properties of asceptic milk and creams. In asceptic processing and packaging of foods of an IUFOST symposium. Step. 19-12.
  62. Harnulv, B. C. and Kandasamy. C. 1981. IDT-symposium on bacteriological quality of raw milk. Part II. P. 47 (cited from Kitchen, B. J. 1985. Elsvier Applied Science Publishers, London).
  63. Hartley, J. C., Vedamuthu, E. R. and Reinbold, G. M. 1969. Bacteriological methods for evaluation of raw milk quality. A review. II. Bacterial tests used to measure milk quality. J. Milk Food Technol. 32:4-15. https://doi.org/10.4315/0022-2747-32.1.4
  64. Harwalker, V. R. 1982. Age gelation of sterilized milks in developments in dairy chemistry-I. D. F. Fox, ed. Applied Science Publishers, London.
  65. Hening, J. C. and Dahlberg, A. C. 1943. Effect of pasteurization times and temperatures on certain properties and constituents of cream. Tech. Bull. N.Y. Agric. Exp. sta. No269:3-23.
  66. Herrington, B. L. 1954. Lipase: A review. J. Dairy Sci. 38:775-789.
  67. Hicks, C. L. 1980. Occurrence and consequence of superoxide dimutase in milk products: A review. J. Dairy Sci. 63:1199-1204. https://doi.org/10.3168/jds.S0022-0302(80)83065-7
  68. Holbrook, J. and Hicks, C. L. 1978. Variation of superoxide dismutase in bovine milk. J. Dairy Sci. 61:1072-1077. https://doi.org/10.3168/jds.S0022-0302(78)83688-1
  69. Janolino, V. G. and Swaisgood, H. E. 1975. Isolation and characterization of sulfhydryl oxidase from bovine milk. J. Biol. Chem. 250:2532-2538.
  70. Jellma, A., and Schipper, C. J. 1975. Influence of physiological factors on the lipolytic susceptibility of milk. Annu. Bull. Int. Dairy Fed. Doc. No. 86. 2.
  71. Jenness, R. and Patton, S. 1959. Principles of dairy chemistry. John Wiley & Sons Inc. New York.
  72. Jonsson, U. and Snygg, B. G. 1974. Lipase production and activity as a function of incubation time, pH and temperature of four lipolytic microorganism. J. Appl. Bacteriol. 37:571-581. https://doi.org/10.1111/j.1365-2672.1974.tb00482.x
  73. Juffs, H. S., Hayward, A. C. and Doelle, H. W. 1968. Growth and proteinase production in Pseudomonas species cultivated under various conditions of temperature and nutrition. J. Dairy Res. 35:385-393. https://doi.org/10.1017/S0022029900019130
  74. Kahn, I. M., Dill, C. W., Chandon, R. C. and Shahani, K. M. 1967. Production and properties of the extracellular lipase of Achromobacter lipolyticum. Biochem. Biophys. Acta. 132:68-77.
  75. Kaminogawa, S., Mizobuchi, H. and Yamauchi, K. 1972. Comparison of bovine milk protease with plasmin. Agric. Biol. Chem. 36:2163-2167. https://doi.org/10.1080/00021369.1972.10860538
  76. Kaminogawa, S. and Yamauchi, K. 1972a. Decomposition of ${\beta}$-casein by milk protease. Similarity of decomposed products to temperature-sensitive and ${\kappa}$-caseins. Agric. Biol. Chem. 36:255-260.
  77. Kaminogaw, S., and K. Yamauchi. 1972b. Acid protease of bovine milk. Agric. Biol. Chem. 36: 2351-2356. https://doi.org/10.1080/00021369.1972.10860582
  78. Kiermeir, F. and Hundt, D. 1969. Uber die ribonuclease der milch, Z. Lebensmithelanters, U-Forsch, 141(2):76-84. https://doi.org/10.1007/BF01291853
  79. Kishonti, E. and Sjostrow, G. 1970. Influence of heat resistant lipases and proteases in psychrotrophic bacteria on product quality. XV III Int. Dairy Congr. IE:501.
  80. Kitchen, B. J. 1976. Enzymatic methods for estimation of the somatic cell count in bovine milk. 1. Development of assay techniques and a study of their usefulness in evaluating the somatic cell content of milk. J. Dairy Res. 43:251-258. https://doi.org/10.1017/S0022029900015806
  81. Kitchen, B. J. 1981. Review of the progress of dairy science: Bovine mastitis milk compositional changes and related diagnostic tests. J. Dairy Res. 48:167-188. https://doi.org/10.1017/S0022029900021580
  82. Kitchen, B. J. 1985. Indigenous milk enzymes. In development in dairy chemistry-3. P. T. Fox, ed. Elsevier Applied Science Publishers, London.
  83. Kitchen, B. J., Taylor, G. C. and White, I. C. 1970. Milk enzymes-their distribution and activity. J. Dairy Res. 37:279-288. https://doi.org/10.1017/S0022029900013339
  84. Klockers, M. and Roberts, P. 1976. Stimulation of phagocytosis human lysozyme. Acta Haemat. 55:289-295. https://doi.org/10.1159/000208029
  85. Knoop, A. M. and Peters. R. H. 1975. Phosphataseaktivitat in sauermilch. Milchwissenschaft 30:674-680.
  86. Korenblat, P. E., Rothbreg, R. M., Minden, P. and Farr, Res. 1968. Immune responses of human adults after oral and parenteral exposure to bovine serum albumin. J. Allergy. 41:226-235. https://doi.org/10.1016/0021-8707(68)90046-4
  87. Korycka-Dahl, M., Dumas, B. R., Chene, N. and Martal, J. 1983. Plasmin activity in milk. J. Dairy Sci. 66:704-711. https://doi.org/10.3168/jds.S0022-0302(83)81848-7
  88. Korycka-Dahl, M., Richardson, T. and Hicks, C. L. 1979. Superoxide dimutase activity in bovine milk serum. J. Food Prot. 42:867-871. https://doi.org/10.4315/0362-028X-42.11.867
  89. Kroll, R. G. 1985. The cytochrome C. oxidase test for the rapid detection of psychrotrophic bacteria in milk. J. Appl. Bacterol. 59:137-141. https://doi.org/10.1111/j.1365-2672.1985.tb03312.x
  90. Kroll, S. and Klostermeyer, H. 1984. Heat inactivation of exogenous proteinase from Pseudomonas fluorescens. 1. Possibility of inactivation in milk, Zeitschrift fur Lebensmittei-Untersuchung und-Forschung. 179:288-295. https://doi.org/10.1007/BF01830430
  91. Kroll, R. G. and Rodrigues, U. M. 1986. Prediction of the keeping quality of pasteurized milk by the detection of cytochrome C oxidase. J. Appl. Bacteriol. 60:21-27. https://doi.org/10.1111/j.1365-2672.1986.tb01060.x
  92. Low, B. A., Andrews, A. T. and Sharpe, M. E. 1977. Gelation of UHT sterilized milk by proteinase from a strain of Pseudomonas fluorescens isolated from raw milk. J. Dairy Res. 44:145-148. https://doi.org/10.1017/S0022029900020057
  93. Low, B. A., Sharp, M. E. and Champman, H. R. 1976. The effect of lipolytic gramnegative psychrotrophs in stored milk on the development of rancidity in Cheddar cheese, J. Dairy Res. 43:459-468. https://doi.org/10.1017/S0022029900016046
  94. Ledford, R. A., Senyk, G. F., Shape, W. F., Kostides, E. and Wolf, E. T. 1983. Influence of growth of uniforms on flavor acceptability of commercially processed milk samples. J. Dairy Sci. 66:1611-1615. https://doi.org/10.3168/jds.S0022-0302(83)81982-1
  95. Leytas, S. P., Bowles, L. K., Komisky, J. and Mangel, W. F. 1981. Activation of plasminogen to plasmin by a protease associated with the outer membrane of Escherichia coli. Proc. Nat. Acad. Sci. U.S.A. 78:1485-1489.
  96. Linden, G. and Alas, C. 1976. Phosphatase alcaline du lait de vache. II. Structure sous-unitaire, nature metalloproteique. Biochim. Biophys. Acta. 429:205-213. https://doi.org/10.1016/0005-2744(76)90043-7
  97. Lodirova, R. and Jouja, V. 1977. Influence of oral lysozyme administration on serum immunoglobulin and intestinal secretory IgA levels in infants. Acta Paediatr. Scand. 66:709-712. https://doi.org/10.1111/j.1651-2227.1977.tb07976.x
  98. Lorrient, D. and Linden, G. 1976. Moving boundary electro-phoresis of native and rennet-treated casein micelles. J. Dairy Res. 43:27-36. https://doi.org/10.1017/S0022029900015569
  99. Malik, A, C. and Swanson, A. M. 1974. Heat stable proteases from psychrotrophic bacteria in milk. J. Dairy Sci. 57:591.
  100. Malik, R. K. and Mathur, D. K. 1984. Purification and characterization of heat-stable protease from Pseudomonas sp. B-25. J. Dairy Sci. 67:522-530. https://doi.org/10.3168/jds.S0022-0302(84)81335-1
  101. Mangino, M. E. and Brunner, J. R. 1976. Two rapid and improved techniques for chromatographic fraction of casein. J. Dairy Sci. 59:153-160. https://doi.org/10.3168/jds.S0022-0302(76)84169-0
  102. Mangino, M. E. and Brunner, J. R. 1977. Isolation and partial characterization of xanthine oxidase associated with milk fat globule membrane of cow's milk. J. Dairy Sci. 60:841-850. https://doi.org/10.3168/jds.S0022-0302(77)83952-0
  103. Marouardt, R. R. and Forster, T. L. 1965. Milk ${\alpha}$-esterase levels as influenced by stage of lactation. J. Dairy Sci. 48:1526-1531. https://doi.org/10.3168/jds.S0022-0302(65)88512-5
  104. Marshall, R. T. and Marstiller, J. K. 1981. Unique response to heat of extracellular protease of Pseudomonas fluorescens M5. J. Dairy Sci. 64:1545-1550. https://doi.org/10.3168/jds.S0022-0302(81)82723-3
  105. Marther, I. H. and Keenan, T. W. 1975. Studies on the structure of milk fat globule membrane. J. Membr. Biol. 21:65-85. https://doi.org/10.1007/BF01941062
  106. Marther, I. H., Tamplin, C. B. and Irving, M. G. 1980. Seperation of the proteins of bovine milk-fat-globule membrane by electrofocusing with retention of enzymatic and immunological activity. Eur. J. Biochem. 110:327-336. https://doi.org/10.1111/j.1432-1033.1980.tb04871.x
  107. McCarthy, R. D. and Long, C. A. 1976. Bovine milk intake and xanthine oxidase activity in blood serum. J. Dairy Sci. 59:1059-1062. https://doi.org/10.3168/jds.S0022-0302(76)84323-8
  108. Mckellar, R. C. 1981. Development of off-flavors in ultrahigh-temperature and pasteurized milk as a function of proteolysis. J. Dairy Sci. 64:2138-2145. https://doi.org/10.3168/jds.S0022-0302(81)82820-2
  109. Morton, R. K. 1985. Alkaline phosphatease of milk. 2, Purification of the enzyme. Biochem. J. 55:795-800.
  110. Mottar, J. 1981. Heat resistant enzymes in UHT milk and their influence on sensoric changes during uncooled storage. Milchiwissenschaft. 36(2):87-91.
  111. Mottar, J. G., Waes, R., Moermons, M. and Naudts, M. 1979. Sensoric changes in UHT milk during uncooled storage. Michi-Wissenschaft 34(5):257-262.
  112. Muir, D. D., Kelly, M. E., Phillips, J. D. and Wilson, A. G. 1978. The quality of blended raw milk in creameries in south west scotland. J. Soc. Dairy Technol. 31:137 (cited from Bassette, R., Fung, D. Y. C. and Mantha, V. R. 1986. CRC critical reviews in Food Sci. Nutr. 24(1):1-52).
  113. Mullen, J. E. C. 1950. The acid phosphatase of cows' milk. I. Some properties of the enzyme. J. Dairy Res. 17:288-305. https://doi.org/10.1017/S0022029900005847
  114. Nelson, J. A. and Trout, M. G. 1965. Judging dairy products. 4th ed, Olsen publishing, Milwaukee Wis.
  115. Noomen, A. 1975. Proteolytic activity of milk protease in raw and pasteurized cow's milk. Neth. Milk and Dairy J. 29:153-161.
  116. Oster, K. A. 1971. Plasmalogen diseases: a new concept of the etiology of the atherosclerotic process. Am. J. Clin. Res. 2:30-35.
  117. Overcast, W. W., and Skean, J. D. 1959. Growth of certain lipolytic microorganisms at $4^{\circ}C$, and their influence on free fat acidity and flavor of pasteurized milk. J. Dairy Sci. 2:1479-1485.
  118. Patel, G. B. and Blankernagel, G. 1972. Bacterial counts of raw milk and flavor of the milk after pasteurization and storage. J. Milk Food Technol. 35(4):203-206. https://doi.org/10.4315/0022-2747-35.4.203
  119. Peer eboom, J. W. C. 1968. Studies on alkaline milk phosphatase. II. Occurrence of various phosphatase isozymes in dairy. Neth Milk Dairy J. 22:137-152.
  120. Phillips, J. D. and Griffiths, M. W. 1987. A note on the use of the catalasemetre in assessing the quality of milk. J. Appl. Bacteriol. 62: 223-226. https://doi.org/10.1111/j.1365-2672.1987.tb02402.x
  121. Pinheiro, A, J. R., Liska, B. J. and Parmellee, C. E. 1965. Heat stability of lipases of selected psychrotrophic bacteria in milk and purdue swiss-type cheese. J. Dairy Sci. 48(7):983-984. https://doi.org/10.3168/jds.S0022-0302(65)88372-2
  122. Polis, B. D. and Shmukler, H. W. 1953. Crystalline lactoperoxidases. Isolation by displacement chromatography, physicochemical and enzymatic properties. J. Biol. Chem. 201:475-500.
  123. Rambauts, W. A., Scharoeder, W. A. and Morrison, M. 1967. Bovine lactoperoxidase. Partial characterization of the further purified protein. Biochemistry. 6:2965-2977. https://doi.org/10.1021/bi00862a002
  124. Reiter, B. 1985, The biological significance of the nonim-munoglobulin protective proteins in milk: lysozyme, lactoferrin, lactoperoxidase. In Development in dairy Chem.-3. Fox. ed, Elsiver Applied Science Publisher, London.
  125. Richardson, B. C. 1983. The proteinase of bovine milk and the effect of pasteurization on their activity. New Zealand Dairy Sci. and Technol. 18:233-245.
  126. Roberts, W. M. 1943. Some factors influencing the spontaneous development of oxidized flavor in milk. Ph. D. thesis, Univ of Minnesota, U.S.A.
  127. Shahani, K. M. and Chandan, R. C. 1965. Activity of purified lipase in the presence of milk constituents. Arch. Biochem. Biophys. 111:257-263. https://doi.org/10.1016/0003-9861(65)90186-4
  128. Shamsuzzaman, K., Molder, W. and Mckellar, R. C. 1987. Survival of lipase during manufacture of non fat dry milk. J. Dairy Sci. 70:746-751. https://doi.org/10.3168/jds.S0022-0302(87)80069-3
  129. Sievers, G. 1981. Structure of milk lactoperoxidase. Evidence for a single polypeptide chain. FEBS Lett. 127:253-256. https://doi.org/10.1016/0014-5793(81)80217-7
  130. Singh, R. R. B. and Patil, G. R. 1987. Physico-chemical and sensory changes during processing and storage of UHT milk. Indian Dairyman. 39(5):209-214.
  131. Skean, J. D. and Overcast, W. W. 1960. Changes in the paper electrophoretic protein patterns of refrigerated skimmilk accompanying growth of three Pseudomonas species. Appl. Microbiol. 8:335. (Cited from Bassette, R., Fung, D. Y. C. and Mantha, V. R. 1986. CRC Critical Reviews in Food Sci. Nutrition. 24(1):1-52).
  132. Skudder, D. J., Thomas, E. L., Pavey, S. A. and Perkin, A. G. 1981. Effects of adding potassium iodate to milk before UHT treatment. I. Reduction in the amount of deposit on the heated surfaces. J. Dairy Res. 48:99-113. https://doi.org/10.1017/S0022029900021518
  133. Snoeren, T. H. M., Van der Spek, C. A., Decker, R. and Both, P. 1979. Proteolysis during the storage of UHT sterilized whole milk. 1. Expriments with milk heated by the direct system for 4 seconds at $142^{\circ}C$. Neth. Milk Dairy J. 33:31-39.
  134. Snoeren, T. H. M., Van Riel, J. A. and Both, P. 1980. Some properties of milk proteinase isolated from UHT milk. Zuivelzicht. 72:42-43.
  135. Snoeren, T. H. M. and Both, P. 1981. Proteolysis during the storage of UHT-sterilized whole milk. 2. Experiments with milk heated by indirect system 4 sec. at $142^{\circ}C$. Neth. Milk Dairy J. 35:113-120.
  136. Stannard, D. J. 1975. The use of marker enzymes to assay the churning of milk. J. Dairy Res. 42:241-246. https://doi.org/10.1017/S0022029900015272
  137. Stepaniak, L. and Fox, P. F. 1983. Thermal stability of an extracellular proteinase from Pseudomonas fluorescens AFT36 J. Dairy Res. 50:171-184. https://doi.org/10.1017/S0022029900022974
  138. Sundhein, G., Zimmer, T. L. and Astrup, H. N. 1983. Induction of milk lipolysis by lipoprotein components of bovine blood serum. J. Dairy Sci. 66:400-406. https://doi.org/10.3168/jds.S0022-0302(83)81806-2
  139. Swaisgood, H. E. 1980. Sulphydryl oxidase: Properties and applications. Enzyme Microbiol. Technol. 2:265-272. https://doi.org/10.1016/0141-0229(80)90095-2
  140. Swaisgood, H. E. and Abraham, P. 1980. Oxygen activation by sulfhydryl oxidases and the enzyme's interaction with peroxidase. J. Dairy Sci. 63:1205-1210. https://doi.org/10.3168/jds.S0022-0302(80)83066-9
  141. Vainio, O. P., Virtanen, J. A. and Kinnuren, P. K. 1982. Inhibition of lipoprotein lipase by benzene boronic acid: Effect of apolipoprotein C-II. Biochim. Biophys. Acta. 711:386-390. https://doi.org/10.1016/0005-2760(82)90051-0
  142. Walker, W. A., and Isselbacher, K. J. 1974. Uptake and transport of macromolecules by the intestine. Possible role in clinical disorders. Gastroenterology. 67:531-550.
  143. Walstra, P. and Jenness, R. 1984. Dairy chemistry and physics. John Willey & Sons, New York.
  144. Warner, R. C. and Polis, E. 1945. On the presence of a proteolytic enzyme in casein. J. Am. Chem. Soc. 67:529-522. https://doi.org/10.1021/ja01220a010
  145. West, F. B., Adams, D. M. and Speck, M. L. 1978. Inactivation of heat resistant protease in normal ultra-high temperature sterilized skimmilk by a low temperature treatment. J. Dairy Sci. 61:1078-1084. https://doi.org/10.3168/jds.S0022-0302(78)83689-3
  146. Whitney, R. M. 1958. The minor proteins of bovine milk. J. Dairy Sci. 41:1303-1323. https://doi.org/10.3168/jds.S0022-0302(58)91096-8
  147. Witter, L. D. 1961. Heat stability of lipases of selected psychrophilic bacteria in milk and purdue-swiss type cheese. J. Dairy Sci. 44:983-987. https://doi.org/10.3168/jds.S0022-0302(61)89851-2
  148. Wuthrich, S., Richterich, R. and Hostettler, H. 1964. Unterschungen uber Milchenzyme. II. Mitteilung. Enzyme in zentrifugerter und hitzebehandelter Kuhnilch. Z, Lebensmittuntersuch. 124(5):345-348.
  149. Zikakis, J. P. and Woosters, S. C. 1980. Activity of xanthine oxidase in dairy products. J. Dairy Sci. 63:893-904. https://doi.org/10.3168/jds.S0022-0302(80)83023-2