臺灣博碩士論文加值系統

摘要
為了開發鋸峰齒鮫作為煉製品加工用之原料，將已凍結貯藏二個月的鋸峰齒鮫分別在-20℃下經1、2、3、4、5、6個月凍藏，解凍後加工製成煉製品。測定其魚肉中鹽溶性蛋白量、鈣核苷三磷酸酶活性及總硫氫基和可反應硫氫基之含量變化情形以及進行煉製品膠強度、白度及品質之試驗。實驗結果顯示，隨著凍藏時間之增加，其鹽溶性蛋白量、鈣核苷三磷酸酶活性分別由62.31mg/g和74.77μmole pi/min/10g降至26.34mg/g及29.24μmole pi/min/10g，又總硫氫基與可反應硫氫基含量亦有隨之下降的現象。鋸峰齒鮫魚漿會隨著凝膠溫度及時間的增加蛋白酶比活性也會隨之增加。其煉製品最適成膠條件則為4℃，13小時魚肉膠強度達到最高值，151.5 g•cm，其曲折試驗可達A-B級。添加不同澱粉含量對魚漿製品膠強度的影響，發現以15%的馬鈴薯澱粉添加量時其膠強度可達最高值，曲折試驗可達A級。而冷凍變性抑制劑的保護試驗結果中發現蔗糖、山梨醇效果最為顯著。

Abstract
In order to develope blue shark (Prionace glauca) as material for processing kamaboko, 2 months frozen storage fish was stored at -20℃ for 1, 2, 3, 4, 5 and 6 months, and then took out for thawing and processing into kamaboko. The salt soluble protein, Ca++-ATPase and protease activity, total-SH and reactive-SH of fish muscle were monitored. And the quality, gel-strength and whiteness, of kamaboko were also determined. From the results, it was found that the salt soluble protein and Ca++-ATPase activity were decressing with storage time extension, from 62.31 mg/g and 74.77μmole pi/min/10g to 26.34 mg/g and 29.24μmole pi/min/10g, respectively. The protease specific activity gradually increased as setting temperature increase and time extension. And the optimal gel-forming condition of fish meat was found setting at 4℃, 13 hurs; the gel strength of kamaboko reached to the best level, 151 g•cm, and its folding test was A-B grade at the same time. It was also found that 15% of potato starch was the optimal quantity for adding into fish paste to produce kamaboko, and the sucrose and sobitol were the best cryoprotectants of this fish.

目 錄
中文摘要…………………………………………………………………1
英文摘要…………………………………………………………………2
壹、前言…………………………………………………………………3
貳、文獻整理……………………………………………………………5
2.1鯊魚肉之一般組成分………………………………………………..5
2.2鯊魚肉質之黏性……………………………………………………..6
2.3魚肉煉製品之製造原理……………………………………………..6
2.4魚肉煉製品的品質判定……………………………………………..7
2.5凝膠與熱解膠………………………………………………………..8
2.6魚肉肉糊成分對凝膠的影響………………………………………..9
2.6.1水分與漂洗…………………………….…………………………...9
2.6.2食鹽的影響……………………….……………………………….10
2.6.3 pH值的影響………………………………………………………11
2.7魚肉蛋白質的熱變性……………………………………………….12
2.7.1凝膠構成的蛋白質………………………………………………..12
2.7.2 Actomyosin-ATPase之熱失活…………………………………...12
2.8鮮度判定法………………………………………………………….13
2.8.1官能方法…………………………………………………………..13
2.8.2化學方法…………………………………………………………..13
(1)以魚肉成分分解生成物為指標………………………………14
(2)以蛋白質變性為指標的方法…………………………………14
2.8.3物理方法…………………………………………………………14
2.8.4微生物學方法……………………………………………………15
3. 冷凍變性抑制劑……………………………………………………15
3.1磷酸鹽類……………………………………………………………16
3.2有機化合物…………………………………………………………16
3.3冷凍變性抑制劑之作用機制………………………………………17
參、實驗藥品與儀器…………………………………………………..18
一、實驗材料…………………………………………………………..18
二、試藥………………………………………………………………..18
三、儀器………………………………………………………………..19
肆、實驗步驟方法……………………………………………………..20
(1)煉製品之製備…………………………………………………20
(2)凝膠強度之測定………………………………………………20
(3)肌動凝蛋白抽出………………………………………………20
(4)肌動凝蛋白之濃度，Ca-ATPase活性分析………………….21
(5)肌動凝蛋白可反應硫氫基含量之測定………………………22
(6)蛋白酶的活性測定……………………………………………22
(7)統計分析………………………………………………………23
伍、結果與討論………………………………………………………..24
一、鋸峰齒鮫魚漿凝膠溫度與時間對產品膠強度之影響…………..24
二、澱粉對鋸峰齒膠肉煉製品品質之影響………………………….25
(1)膠強度………………………………………………………….25
(2)色澤…………………………………………………………….26
三、凍藏對水鯊魚肉凝膠能力的影響………………………………..27
四、冷凍變性抑制劑對鋸峰齒鮫煉製品品質之影響………………..28
(1)蔗糖、山梨醇、菊糖在凍藏期間對肌動凝蛋白之影響…….28
(2)蔗糖、山梨醇、菊糖在凍藏期間鈣核苷三磷酸酶活性之影響
..………………………………………………………………...28
(3)蔗糖、山梨醇、菊糖在凍藏期間肌動凝蛋白總硫氫基與可反
應硫氫基之影響……………………………………………….28
(4)蔗糖、山梨醇、菊糖在凍藏期對煉製品膠強度之影響…….29
陸、結論………………………………………………………………...30
柒、參考文獻……………………………………………………………31
圖………………………………………………………………………..39
表………………………………………………………………………..49

柒、參考文獻
于名振，1986，臺灣脊椎動物誌，P.69，臺灣商務印書館發行。
吳清熊，1991，臺灣水產加工業現況，P.88 ，臺灣省漁業局發行。
姜文媚、龔鳴盛，1992，阿根廷魷魚在擂潰和靜置中蛋白質穩定性對成膠能力之影響。食品科學，19(2) : 264-277.
祝永平，1993，以示差掃瞄熱量分析技術探討淡水吳郭魚魚漿的成膠機構。國立台灣海洋大學食品科學研究所碩士論文。
謝榮峰，1999，微生物轉麩胺酸醯胺基酶之量產最適條件及其在水產煉製品中的應用。國立台灣海洋大學食品科學研究所碩士論文。
孫朝棟，魚署魚漿冷凍時水分動態與功能特性之關係。國立台灣大學博士論文。
孫寶年、李國皓、翁秀貞，1986，臺灣地區常見食用魚貝類圖說， P.75，行政衛生署編印。
孫寶年、徐仁鏤、李錦楓，1980，單寧酸對煉製品彈性之影響。食品科學，7(1): 22。
鄭森雄，1977， 臺灣水產加工業實況，P.118，農業復興委員會發行。
志水寬、元應輝重、秋場稔、外山健三，1988， 水產加工，P.563-576，講談社，東京。
佐久間 利男，1985，凍結乾燥食品之品質保持。食品科學，27(11): 82-91。
須山三千三、鴻巢章二(1987)，水產食品學，P.48，恆星社厚生閣 ，東京。
An, H., Weerasinghe, V., Seymour, T. A. and Morrissey, M. T. 1994. Cathepsin degradation of Pacific whiting surimi proteins. J. Food Sci. 59: 1013-1017.
Aria, K., Takashi, R. and Saito, T. 1970. Studies on muscular proteins of fish III, Inhibition by sorbitol and sucrose on the denaturation of carp actomyosin during frozen storage. Bull. Jap. Soc. Sci. Fish. 36: 232
Arai, K., Kawamura K., and Hayashi, C. 1973. The relative thermo-Stabilities of the actomyosin-ATPase from the dorsal muscles of various fish species. Bull. Jap. Soc. Sci. Fish. 39: 1077.
Arai, K. 1974. Evaluation of fish quality from the muscle protein studies. In “Quality of Fish”, P.55-80, ed. by Jap. Soc. Sci., Koseisha, Tokyo.
Asghar, A., Samejima,K,and Yasui, T.1984. Functionalty of muscle proteins in gelation mechanisms of structured meat prooducts. CRC Critical Reviews in Food Sciene and Nutrition. 22(1): 27-106﹒
Geis, A., Bockelmann, W. and Teuber, M. 1985. Simultaneous extraction and purification of a cell wall-associated peptidase and β-casine specific protease from Streptococcus cremoris ACl. Appl Microbiol Biotechnol. 23: 79-84.
Chen, C. S., Hwang, D. C., and Jiang, S. T. 1988. Purification and characterization of milkfish myosin. Nippon Suisan Gakkaishi. 54: 1423-1427.
Chow, C.J. (1984), Studies on the texture change during frozen stage for minced fish product, J . Fish. Soc. Taiwan. 11: 37.
Conell, J. J. 1960. Changes in the adenosine triphosphatase acitivity and sulphydryl group of cod flesh during frozen strotage. J. Sci. Food Agric. 11: 245.
Franks, F. 1975. Water, ice and solutions of simple molecules. In “Water Relstion of Foods”, P3-22, ed. by Duckworth, R. B. Academic Press, London.
Hashimoto, A., Kobayashi, A., and Arai, K. 1982. Thermostability of fish myofibrillar Ca-ATPase and adapation to environmental tempetature. Bull. Jap. Soc. Sci. Fish. 48: 671.
Ishioroshi, M., Samejima, K., and Yasue, T. 1979. Heat inducd gelation of myosin. J. Food Sci. Fish. 48: 671.
Itoh, Y., Yoshinaka, Y. and Ikeda, S. 1980. Formation of polymeric molecules resulting from the intermolecular SS bond formation during gel formation of carp actomyosin by heating. Bull. Japan Soc. Sci. Fish. 46: 621-624.
Iwata, K., Kanna, K., Vmemoto, S., and Okada, M. 1971. Study of the guality of frozen stroed Alaska pollock surimi. I. The influence of freshness of the material and change in storage temperate. Bull. Jap. Soc. Sci. Fish. 37: 26.
Iwata, K., Kobashi K., and Hase, J. 1974. Studies on muscle alkaline protease. II. Some enzymatic properties of carp muscular alkaline protease. Bull. Jap. Soc. Sci. Fish. 40: 189.
Iwata, K., Kobashi K., and Hase, J. 1977. Studies on muscle alkaline protease. VI. Purification of proteins which induce the “modori” phenomenon during kamaboko production and cathepson A from carp muscle . Bull. Jap. Soc. Sci. Fish. 43: 181.
Jiang, S. T., Hwang, C. D., and Tsao, C. Y., 1987. Functionality changes in myofibrillar proteins of milkfish during icing . XVIIth International Congress of Refrigeration. P.534-549.
Jiang, S. T., Lee, J. J. and Chen, H. C. 1996. Proteolysis of Actomyosin by Cathepsins B, L, L-like and X from mackerel (Scomber australasicus). J. Agric. Food Chem. 44: 769-773.
Jiang, S. T., San, P. C. and Japit, L. S. 1989. Effect of storage temperatures on the formation of disulfides and denaturation of tilapia hybrid actomyosin. J. Agric. Food Chem. 37(5): 1228-1231.
Kanon, S. Watabe, S. and Hashimoto, K. 1983. Isolation and some physicochemical properties of requiem shark myosin, Bull. Jap. Soc. Sci. Fish. 49(5): 757-763.
Kawashima, T., Arai, K. and Saito, T. 1973. Stuides on musclar protein of fish-X. The amount of actomyosin in frozen “ surimi” from alaska-pollack. Bull. Jap. Soc. Sci. Fish. 51: 53.
Kim, B. Y., Hamann, D. D., Lanier, T. C. and Wu, M. C. 1986. Effects of freeze-thaw abuse on the viscosity and gel-formation properties of surimi from two species. J. Food Sci. 51: 951-956.
Koreeda, N., Ishigami,T. and Fujita,K(1982), Kamaboko-iorming capacity of shark meat.Bull. Jap. Soc. Sci. Fish. 48(12): 1815-1819.
Kudo, G., Okada, M. and Miysuchi, D. 1973. Gel-formation capacity of washed and unwashed flesh of some Pacific coast species of fish. Mar. Fish. Rev. 35: 10-15.
Laemmli, U. K. 1970. Cleavage of structure proteins during the assembly of the head of bacteriophage T4. Nature 277. 680-685.
Lanier, T. C. 1988. Muscle protein funtional properties and protease content of surimi prepared from fatty, dark-fleshed fish species. Proc. Intl. Conf. Fatty fish Utilization: Upgrading from Feed to Food. Raleigh, NC, UNC Sea Grant Publ. 88-04. P. 247.
Lee, C. M. 1984. Surimi process technology. Food Technology. 38(10): 69.
Linko, R. R. and Nikkila, O. E. 1961. Inhibition of the denaturation by salt of myosin in Baltic herring. J. Food Sci. 20: 606.
Lippincott, R. K., and Lee , C. M. 1983. Factors attecting gel characteristics of red hake surimi. Presented at 43rd Ann. Meeting of Inst. of Food Technologist, New Orleans, La., June 19-22.
Makinodan, Y. and Ikeda, S. 1971. Studies on fish muscle protease. IV. relation between himodori of kamaboko and muscle protease. Bull. Jap. Soc. Sci. Fish. 37: 518.
Matsumoto, J. J. and Noguchi, S. 1971. Proc. Int. Congr. Refrig. 13th. Vol. 3:237 cited by Matsumoto, J. J.(1980)
Matsumoto, J. J. 1979. Denaturation of fish muscle proteins during frozen storage. In “Protein at Low Tempture” P.205-224, ed. by Fennma, O., ACS Sympo. Series 180, ACS Washington D. C.
Matsumoto, I., Ooizumi, T. and Arai, K. 1985. Protective effect of sugar freeze-denaturation of carp myofibrillar protein. Bull. Jap. Soc. Sci. Fish. 51: 833.
Matsuda, Y. 1979. Influence of sugars on the protein denaturation of lyophilized carp myofibrils during storage.
Matsura, M. and Arai, K. 1987. Preparation properties of myosin native thick filaments from fish dorsal muscle. Nippon Suisan Gakkaishi. 53: 1073.
Morioka, K. and Shimizu, P. 1990. Contribution of sarcoplasmic protein to gel formation of fish meat. Hippon Suisan Gakkaishi. 56: 929.
Murozuka, T., Takashi, R., and Arai, K. 1976. Relative thermostabilities of Ca-ATPase of myosin and actomyosin from Tilapia and rabbit. Bull. Jap. Soc. Sci. Fish. 42: 5.
Murozuka, T. and Arai, K. 1976. Purification and thermostability of myosin Ca-ATP from the frozen muscle of yellowfin tuna. Bull. Jap. Soc. Sci. Fish. 42: 65.
Niwa, E., Suzuki, M. and Nakayama, T. 1985. Heat-induced polymerization of fish actomyosin. Bull. Jap. Soc. Sci. Fish. 51: 1795.
Niwa, E., Wang, T. T., Kanoh, S. and Nakayama, T. 1988. Strength effect of the various natural high polymers on elasticity of the kamaboko. Nippon Suisan Gakkaishi. 54(4): 541-588.
Noguchi, S. and Matsumoto, J. J. 1970. Studies on the control of the denaturation of the fish muscle proteins during frozen stroage I. Bull. Jap. Soc. Fish. 36: 1078.
Noguchi, S. and Matsumoto, J. J. 1970. Studies on the control of the denaturation of the fish muscle protein during frozen storage. Bull. Jap. Soc. Sci. Fish. 37: 1115.
Noguchi, S. 1974. The control of denaturation of fish muscle proyeins during frozen storage. Doctoral Dissertation. Sophia Univ., Tokyo, Japa.
Noguchi, S. Oosawa, K. and Matsumoto, J. J. 1976. Studies on the control of denaturation of fish muscle proteins during frozen storage VI. Preventive effect of carbohydrates. Bull. Jap. Soc. Sci. Fish. 42: 77.
Nomura, A., Itoh, Y., Nishikawa, S. and Obatake, A. 1994. The gel strengthening effect of two- step heating on the meat pastes fromdifferent fish in modori-inducing conditions. Nippon Suisan Gakkaishi 60: 667.
Oguni, M., Inoue, N., Ohi, K. and Shinano, H. 1987. Denaturation of crap Myosin B during frozen and supercooled storage at -8℃. Nippon Suisan Gakkaish.
Ojima, T. and Nishita, K. 1987. Dissociation of regulatory light chain from hybrid myosin. Nippon Suisan Gakkaishi. 53: 93.
Okada, M. 1963. Studies of elastic property of kamaboko. Bull. Tokai Reg. Fish. Res. 36: 21.
Okada, T., Inoue, N., and Akiba, M. 1986. Electron microscopic observation and biochemical properties of carp myosin B during forzen storage. Bull. Jap. Soc. Sci. Fish. 53: 345.
Park, J. W. 1994. Functional protein additives in surimi gels. J. Food Sci. 59: 525-527.
Shimizu, Y. and Nishioka, F. 1974. Interactions between horse mackerel actomyosin and sarcoplasmic proteins during heat cogulation. Bull. Jap. Soc. Sci. Fish. 40: 231.
Shimizu, Y. and Machida, R., and Takenami, S. 1981. Species variation in the gel-forming chacteristic of fish meat paste. Bull. Jap. Soc. Sci. Fish. 47: 95.
Sikorski, Z., Olley. J. and Kostuch, S. 1976. Protein changes in frozen fish. CRC Critical Reviews in Food Science and Nutrition, Vol. 8, No.1, P.97-129, CRC Press, New York, N.Y.
Sun, Chao-Tung 1981. Water behavior and functionality of frozen Dolphin-fish mince. Doctorate, Dept. Agric. Chem., Natl. Taiwai Univ., Taipai, Taiwan, R.O.C.
Tanikawa, E., Akiba, E., and Shitamori, A. 1963. Cold storage of cod fillets treated with polyphosphate. Food Techno. 17: 1425.
Tanikawa, E., Motohiro, T., and Akiba, M. 1985. Marine Products in Japan. P.337-341. Koseisha koseikaku Co. Ltd, Tokyo.
Taso, C. Y. 1981. Studies on the denaturation of muscle proteins of Mackerel and amberfish during frozen storage. Master’s thesis, Dept. Marine Food Sci., Natl. Taiwan Collage of Marine Sci. & Techno., Taiwan, R.O.C.
Toyohara, H., Sasaki, K., Kinoshita, M., Shimizu, Y. and Sakaguchi, M. 1991. Detection of inhibitors for modri-inducing proteinase in fish and calf serums. Nippon Suisan Gakkaishi. 57: 521-525.
Umemoto, S. 1966. A modified method for estimation of fish muscle Propeins by Biuret Method. Bull. Jap. Soc. Sci. Fish. 32: 427.
Watabe, S. Ochiai, Y. Kanon, S. and Hashimoto, K. 1983. Proximate and protein compositions of requiem shark muscle, Bull. Jap. Soc. Sci. Fish. 49(2): 265-268.
Wu. C. H. 1983. Recovery of protein from the leaching waste water of Frozen surimi by acid coagulaion. Bull. Taiwan Fish. Res. Inst. 35:252.
Wu, M. C., Akahane, T., Lanier, T. C. and Hamann, D. D. Thermal transitions of Actomyosin and Surimi Prepared from Atlantic Croaker as Studied by Differential Scanning Calorimetry. J. Food. Sci. 50(1): 10-13, 1985a.
Wu, M. C., Lanier, T. C. and Hamanin, D. D. 1985. Thermal transitions of admixed starch fish protein systems during heating. J. Food. Sci. 50:20.
Yasui, T., Ishiorodhi, M., Nakano, H. and Samejima, K. 1979. Change in Shear modules; Ultrastructure and spin-spin relaxtion heat induced gelation of myosin. J. Food Sci. 44: 1201.