本實驗主要在探討山羊乳中各種酪蛋白多態性與乳熱安定性之關係。結果顯示無論是場別(國立台灣大學農業試驗場與台南縣林場供試羊乳樣熱安定性平均值分別為13.57±3.56及13.28 ±5.71秒)或品種(Alpine與Saanen供試羊乳樣熱安定性平均值分別為13.51±0.58及13.22±0.93秒)，經統計分析知場別與品種之效應並不顯著(P>0.05)。
供試羊乳樣之各酪蛋白多態性與乳熱安定性之關係探討中，僅發現κ-酪蛋白者具有顯著差異(P<0.05)，以κ-酪蛋白AA型與AB型熱安定性較佳，BB型熱安定性最差；其它酪蛋白多態性間的乳熱安定性則無顯著差異(P>0.05)。故依本實驗之結果，尚無法確定何種酪蛋白多態性組合的羊乳具有最佳的熱安定性。

The purpose of this experiment was to investigate the relationship between the polymorphisms of various caseins and the heat stability of goat milk. The results showed that there were no difference between farms ( NTU farm 13.57±3.56 sec, Lin farm 13.28±5.71 sec) or breeds (Alpine 13.51±0.58 sec, Saanen 13.22±0.93 sec) in heat stability of goat milk (P>0.05).
In the relationship between the polymorphisms of various caseins and the heat stability of goat milk, the results showed only κ-casein had significantly different (P<0.05), κ-casein AA and AB had the best heat-stability of goat milk, the heat stability of κ-casein BB was worse. The heat stability of goat milk among polymorphisms of other caseins was not significant (P>0.05). According to the results of heat stability of goat milk in this experiment, we can not propose to establish the best polymorphisms combination of various caseins.

目次 Ⅰ
表次 Ⅱ
圖次 Ⅲ
壹、摘要 1
貳、緒言 2
參、文獻檢討
一、乳及乳製品製造處理之流程 3
二、乳酪蛋白之特性 7
三、乳加熱條件及乳熱安定性測定之方法 13
四、牛乳及山羊乳加熱之特性 15
五、乳成份與熱安定性之關係 17
六、乳酪蛋白多態性與熱安定性之關係 25
肆、材料與方法 28
伍、結果與討論 38
陸、結論 59
柒、參考文獻 60
捌、英文摘要 70
玖、作者小傳 71

中國國家標準，1987。酸度之測定3441。經濟部。
中國國家標準，1987。比重之測定3442。經濟部。
林炯仁，1999。pp. 36-37。羊協一家親。中華民國養羊協會，嘉義
市。
吳輔佑，2000。pp. 2-6。羊協一家親。中華民國養羊協會，嘉義市。
梁逸，1999。pp. 16-18。羊協一家親。中華民國養羊協會，嘉義市。
梁逸，2000。pp. 26-27。羊協一家親。中華民國養羊協會，嘉義市。
王雅芳，1996。生羊乳中還原牛乳之檢出。國立台灣大學畜產學研
究所碩士論文。
林慶文，1983。酪蛋白膠粒的構造。科學農業31：179-182。
林慶文，1993。乳製品之特性與機能。pp. 37-42。華香園出版社，
台北市。
林慶文，1993。乳品加工學。華香園出版社，台北市。
Anema, S. G. and D. J. Stanley. 1998. Heat-induced, pH-
pependent behaviour of protein in caprine milk. Int. Dairy
Journal 8: 917-923.
Anema, S. G. and H. Klostermeyer. 1997a. Heat-induced, pH-
dependent dissociation of casein micelles on heating
reconstituted skim milk at temperatures below 100 ℃. J.
Agricul. Food. Chemist. 45：1108-1115.
Anema, S. G. and H. Klostermeyer. 1997b. The effect of pH and
heat treatment on the κ-casein content and the potential of
the particles in reconstituted skim milk. Milchwissenschaft
52：217-223.
Antherton, H. V. 1977. Chemistry and testing of dairy products.
4th edition. Avi Publishing Company, Inc. Westport,
Connecticut.
AOAC. 1980. Official methods of analysis, 13th ed. Association
of official analytical chemists. Arlington, VA.Bovenhuis, H.
and A. J. M. Verstege. 1989. Improved method for phenotyping
milk protein variants by isoelectric focusing PhastSystem.
Neth. Milk Dairy J. 43:447-451.
Brignon, G., B. Ribadeau-Dumas, F. Grosclaude, and J. C.
Mercier. 1971. Structure primaire de la caseine β bovine.
Eur. J. Biochem. 22：179-185.
Broderick, G. A. and M. K. Clayton. 1997. A statistical
evaluation of animal and nutritional factors influencing
concentrations of milk urea nitrogen. J. Dairy Sci. 80：2964-
2971.
Chen, P. S., T. Y. Toribara, and H. Warner. 1983.
Microdetermination of phosphorus. Anal. Chem. 28:1756-1758.
Coll, A., J. M. Folch, and A. Sanchez. 1993. Nucleotide
sequence of the goat κ- casein cDNA. J Anim. Sci. 71：2833.
De Peters, E. J. and J. P. Cant. 1992. Nutritional factors
influencing the nitrogen composition of bovine milk：a review.
J. Dairy Sci. 75：2043-2070.
Dennenberg, F. and H. G. Kessier. 1988. Reaction kinetics of the
denaturation of whey proteins in milk. J. Food Sci. 53：259-263.
Donnelly, W. J. 1977. Chromatography of milk proteins on
Hydroxyapatite. J Dairy Res. 44：621-625.
Fox, P. F. 1982. Heat-induced coagulation of milk. In：P. F. Fox. Eds.
Developments in dairy chemistry -Ⅰ. Proteins. pp. 189-228. Applied
Science Publishers, London.
Fox, P. F. and M. C. T. 1976. Heat stability characteristics of ovine,
caprine, and equine milks. J. Dairy Res. 43：433-442.
Fox, P. F. and P. A. Morrissey. 1977. Reviews of progress of dairy science: the heat stability of milk. J. Dairy Res. 44: 627-646.
Fox, P. F. and P. L. H. McSweeney. 1998. Dairy chemisty and
biochemistry. Blackie Academic and Professional, London.
Fox, P. F., M. K. Happer, V. H. Holsinger, and M. J. Pallansch. 1966.
Effects of high-heat treatment on stability of calcium caseinate
aggregates in milk. 33：443-450.
Gough, P. and R. Jenness. 1962. Heat denaturation of β-lactoglobulins
A and B. J. Dairy Sci. 45：1033-1039.
Harding, F. 1995. Milk quality. Blackie Academic and Professional,
London.
Hiller, R. M. and R. L. J. Lyster. 1979. Whey protein denaturation in
heated milk and cheese whey. J. Dairy Res. 46：95-102.
Hiller, R. M., R. L. J. Lyster, and G. C. Cheeseman. 1979. Thermal
denaturation of α-lactalbumin and β- lactoglobulin in cheese
whey：effect of total solids concentration and pH. J. Dairy Res. 46：
103-111.
Jakob, E. and Z. Puhan. 1992. Technological properties of milk as
Influenced by genetic polymorphism of milk proteins-A review.
Int. Dairy journal 2：157-178.
Jandal, J. M. 1996. Comparative aspects of goat and sheep milk. Small
Ruminant Res. 22：177-185.
Jenness, R. 1974. The composition of milk. In:Lactation. B. L. Larson
and V. R. Smith. Eds. Vol. Ⅲ, pp. 3-107. Academic Press, New York.
Jensen, R. G. 1995. Handbook of milk cpmposition. Academic Press,
New York.
Jonker, J. S., R. A. Erdman, and S. M. Andrew. 1997. Estimation and
evaluation of nutritional parameters from milk urea nitrogen. J. Dairy
Sci. 80（Suppl. 1）：85.（Abstr.）
Kaneko, J. J. 1989. Clinical biochemsitry of domestic animals. 4th
edition. Academic Press Inc, New York.
Kim, H. H. Y., and R. Jimenez-Flores. 1994. Comparison of milk proteins
using preparative isoelectric focusing followed by polyacrylamide gel
electrophoresis. J. Dairy Sci. 77：2177-2190.
Kudo, S. 1980. The heat stability of milk：formation of soluble proteins
and protein-depleted micelles at elevated temperatures. Zew Zealand J.
Dairy Sci. Tech. 15：255-263.
Lyster, R. L. J. 1970. The denaturation of α-lactalbumin and β-
lactoglobulin in heated milk. J. Dairy Res. 37：233-243.
Manji, B. and Y. Kakuda. 1986. Thermal denaturation of whey protein in
skim milk. Can. Inst. Food Sci. Technol. J. 19：163-166.
Marshall, R. J. 1986. Effects of jodate, hydrogene peroxide and
dichromate on the denaturation of whey proteins in heated milk. J.
Dairy Res. 53：89-95.
Martin, P. and F. Grosclaude. 1993. Improvement of milk protein quality
by gene technology. Livestock Prod. Sci. 35：95-115.
McKenzie, G. H., R. S. Norton, W. H. Sawyer. 1971. Heat-induced
interaction of β- lactoglobulin and κ- casein. J. Dairy Res. 38：
343-351.
McLean, D. M., E. R. B. Graham., R. W. Ponzon, and H. A. McKenzie.
1987. Effects of milk protein genetic variants and composition on heat
stability of milk. J Dairy Res. 54：219-235.
Melendez, P. A. Donovan, and J. Hernandez. 2000. Milk urea nitrogen
and infertility in Florida Holstein cows. J. Dairy Sci. 83：459-463.
Mercier, J. C., F. Addeo, and J. P. Pelissier. 1976. Structure primaire du
caseinomacropeptide de la caseine κ carpine. Biochimie. 58：1303-
1310.
Miller, P. G. and H. H. Sommer. 1940. The coagulation temperature of
milk as affected by pH, salts, evaporation and previous heat treatment.
J. Dairy Sci. 23：40-421.
Mohammad, K. S. and P. F. Fox. 1987. Heat-induced association-
dissociation of casein micelles preceding coagulation. J. Dairy Res.
54：377-387.
Morand-Fehr, P. 1991. Goat nutrition. Pudoc, Wageningen.
Muir, D. D. and A. W. M. Sweetsur. 1976. The influence of naturally
Occurring levels of urea on the heat stability of bulk milk. J Dairy Res.
43：495-499.
Muir, D. D. and A. W. M. Sweetsur. 1977. Effect of urea on the heat
coagulation of the caseinate complex in skim-milk. J Dairy Res. 44：
249-257.
Mukherjee, D., A. K. Bandyopadhyay, and P. K. Ghatak. 1993. Some
Factors affecting heat stability of goat milk. Indian J. Dairy Sci. 46：
307-310.
O’Connell, J. E. and P. F. Fox. 2000. The two-stage coagulation of milk proteins in the minimum of the heat coagulation time-pH profile of milk: effect of casein micelle size. J. Dairy Sci. 83: 378-386.
Parnell-Clunies, E., Y. Kakude, and D. Irvine. 1988. Heat induced changes in milk processed by vat an continuous heating systems. J. Dairy Sci. 71：1472-1483.
Pyne, G. T. 1958. The heat coagulation of milk. Ⅱ. Variations in sensitivity of casein to calcium ions. J. Dairy Res. 25：467-474.
Pyne, G. T. 1962. Some aspects of the physical chemistry of the salts of milk. J. Dairy Res. 29：101-130.
Pyne, G. T. and K. A. McHenry. 1955. The heat coagulation of milk. J. Dairy Res. 22：60-68.
Recio, I. And C. Olieman. 1996. Determination of denatured serum proteins in the casein fraction of heat-treated milk by capillary zone
electrophoresis. Electrophoresis. 17:1228-1233.
Recio, I., M. L. Perez-Rodriguez, L. Amigo, and M. Ramos. 1997. Study of the polymorphism of caprine milk caseins by capillary
Electrophoresis. 64:515-523.
Recio, I., M. L. Perez-Rodriguez, M. Ramos, and L. Amigo. 1997.
Capillary electrophoretic analysis of genetic variants of milk proteins
from different species. Electrophoresis 768:47-56.
Richardsin, B. C. and L. K. Creamer. 1974. Comparative micelle
structure. Ⅲ. The isolation and chemical characterization of caprine
β1- casein and β2- casein. Biochim. Biophys. Acta 365：133-137.
Roberts, B., P. Di Tullio, J. Vitale, K. Hehir, and K. Gordon. 1992.
Cloning of the goat β- casein-encoding gene and expression in
transgenic mice. Gene 121：255-262.
Robitaille, G. 1995.Influence of κ- casein and β- lactoglobulin genetic
variants on heat stability of milk. J. Dairy Res. 62：593-600.
Rodriguez, L. A., C. C. Stallings, J. H. Herbein, and M. L. McGilliard.
1997. Effect of degradability of dietary protein and fat on ruminal,
blood anf milk components of Jersey and Holsteinc ows. J. Dairy Sci.
80：353-363.
Rose, D. 1961. Factors affecting the pH-sensitivity of the heat stability of
milk from individual cows. J. Dairy Sci. 44: 1405-1413.
Rose, D. 1962. Factors affecting the heat stability of milk. J. Dairy Sci. 45：1305-1311.
Rose, D. 1965. Protein stability problems. J Dairy Sci. 48：139-146.
Rose, D. and H. Tessier. 1959. Composition of utlrafiltrates from milk
heated at 80 to 230 ℉ in relation to heat stability. J. Dairy Sci. 42：
969-980.
Swayer, W. H. 1968. Heat denaturation of bovine β- lactoglobulins and
relevance of disulphide aggregation. J. Dairy Sci. 51：323-329.
Swayer, W. H., R. S. Norton, L. W. Nichol, G. H. McKenzie. 1971.
Thermo-denaturation of bovine β- lactoglobulins. Kinetics and the
Introduction of β- structure. Biochimica et biophysica Acta. 243：
19-30.
Schmidt, D. 1979. G. J. Dairy Sci. 46：351.
Singh, H. and P. F. Fox. 1985. Heat stability of milk：pH-dependent dissociation of micellar κ- casein on heating milk at ultra high temperatures. J. Dairy Res. 52：529-538.
Singh, H. and P. F. Fox. 1987. Heat stability of milk：influence of collidal and soluble salts and protein modification on the pH-dependent dissociation of micellar κ- casein. J. Dairy Res. 54：523-534.
Sweetsur, A. W. M. and J. C. D. White. 1974. Studies on the heat stability of milk protein. Ⅰ. Interconversion of type A and type B milk heat-stability curve. J. Dairy Res. 41：349-358.
Tessier, H. and D. Rose. 1964. Influence of κ- casein and β-
lactoglobulin on the heat stability of skimmilk. J. Dairy Sci. 47: 1047-1051.
Thompson, M. P., R. T. Boswell, V. Martin, R. Jenness, and C. A. Kiddy. 1969. Casein pellet solvation and heat stability of individual cow’s milk. J. Dairy Sci. 52：796-798.
Trujillo, A. J., I. Casals, and B. Guamis. 2000. Analysis of major caprine milk protein by reverse-phase high-performance liquid chromatography and electrospray ionization-mass spectrometry. J. Dairy Sci. 83：11-19.
Tziboula, A. 1997. Casein diversity in caprine milk and its relation to
technological properties: heat stability. Int. J. Dairy. Tech. 50:134-138.
Visser, S. A. 1962. J. Dairy Sci. 45：710.
Williamson, D. H. and J. Medllanby. 1983. D-3-hydroxybutyrate. pp.
1836-1839. In H. U. Bergmeyer. Methods of enzymatic analysis, Vol.
IV, 3th edition. Verlage Chemic, Weinheim.
Zadow, J. G., J. F. Hardham, H. R. Kocak, and J. J. Mayes. 1983. The
stability of goat’s milk to UHT processing. Aus. J. Dairy Tech. 38：
20-23.