臺灣博碩士論文加值系統

本研究擬以進口冷凍金線鰱魚漿為實驗原料。探討其品質之穩定性；製程中魚漿靜置處理條件的最適化及其鹽溶性蛋白質變化機制；以及添加水分和馬鈴薯澱粉配方對煉製品質感的影響。
實驗結果發現，進口SA級魚漿品質優劣性差異極大，經以DSC測試證實不同製備或儲運所造成的魚漿蛋白質凝聚變性，應是最可能導致魚漿品質劣變的原因。兼併地利用DSC和TSRM來測試在靜置處理過程中魚漿之肌動凝蛋白（AM）的變化，可證實正常之金線鰱加鹽擂潰魚漿的AM為自由態的肌動蛋白（A）和肌凝蛋白（M），而經5 ℃及25 ℃靜置的魚漿AM會分別轉化成AM複合體和TGase酵素催化的AM架橋複合體而獲致蒸煮凝膠強度的改善，對應之5 ℃靜置20小時可有效地令魚漿膠強度由無靜置的644 ±15 g-cm提升至791 ±8 g-cm；25 ℃靜置6小時更進一步將魚糕膠強度提升至2200 ± 32 g-cm。
調整配方所生產的魚糕與市販魚丸和魚板產品進行質感比較，發現未經靜置處理者，含水率78 %wc之配方產品與市販一般魚板相似，而水分提高至80 %wc之配方質地近似一般魚板而更具彈性，在高水分之84 %wc配方可得一般市販魚丸。對在蒸煮前有經25 ℃靜置6小時操作者，在廣泛的低含水率76-82 %wc配方範圍均產製出膠強度超越市販高級魚板的強軔質感，僅有在含水率高於80 %wc的配方能獲得與市販高級魚板相同品質的產品。澱粉添加至各含水率所生產之煉製品，穿破力隨水分增加而提高，但變形度並無明顯影響。超過7.5 %添加時，魚糕質地變粗糙而劣化。

The purpose of this research was to survey quality stability of imported frozen threadfin bream surimi, and studies on optimization of setting treatment conditions and mechanism of salt-soluble protein changes in the fish-gel preparation as well as the additives, moisture and potato starch, affection on surimi gel properties.
On stable qualities difference is great were found in surveying on the most SA grade surimi. The low grade surimi was evidence most possibility to be the partial denature due to the improper processing on store. Monitor the major salt-soluble protein, AM changes during setting by DSC and TSRM, it was evidence the AM in free A and M forms was converted to an AM complex and a TGase promote cross link type AM complex to benefit the final fish gel strength during setting. It was found the performing of a 5 oC/20 h setting treatment could improve the gel strength from 644 ±15 g-cm to 791 ±8 g-cm ; 25 oC/6 h setting could result an even phenomenal improve on the product gel strength up to 2200 ±32 g-cm, respectively.
To evaluate the changes of gel product qualities as effected by additives, with comparable to commercial fish ball and kamaboko, for gels prepared without setting treatment additives, kamaboko type product were resulted at a lower moisture content 78 %, resemble kamaboko type product were resulted at 80 % wc, fish ball type product were resulted at a higher moisture content 84 %. For gels prepared with a 25 oC/6 h setting treatment prior to cooking, gel properties tougher then high grade kamaboko was resulted for gels contenting any moisture content between 76-83 %, gels possessing exactly similar properties to high grade kamaboko could only be result at high moisture content between 80-84 %. Addition of potato starch could only increase the breaking force and could not significantly affected the deformation at break, higher then 7.5 % level of starch addition would result gel with unfavorable sandy texture.

目錄

封面內頁 頁次
目錄 i
中文摘要 v
英文摘要 vi
圖目錄 viii
表目錄 x
第一章 前言 1
1.1 研究背景 1
1.2 研究目的 1
1.3 文獻整理 2
1.3.1 肌肉蛋白質之組成 2
（1）肌漿蛋白質 2
（2）肌原纖維蛋白質 2
（3）基質蛋白質 7
1.3.2 魚漿凝膠作用及影響因子 7
（1）Transglutaminase催化反應 7
（2）靜置處理 8
1.3.3 不同肌肉蛋白質之熱分析 9
（1）肌肉態 10
（2）魚漿態 11
（3）單離態 12
1.3.4熱掃描剛性測定儀對魚漿的探討 13

第二章 實驗材料與方法 15
2.1 材料 15
2.2 儀器設備 15
2.3 方法 15
2.3.1 pH值測定 16
2.3.2 水分含量測定 16
2.3.3 魚漿煉製品之製備 16
2.3.4 魚漿煉製品之靜置處理操作 17
2.3.5 添加澱粉之魚糕操作 17
2.3.6 魚漿凝膠製品物性品質測定 17
2.3.7 示差掃描熱分析 18
2.3.8 熱掃描剛性靜置凝膠分析 18

第三章 結果與討論-壹 20
壹、進口冷凍SA級金線鰱魚漿品質調查及兩類型魚漿之發現 20
3.1 未靜置處理 20
3.2 靜置處理 21
3.2.1 低溫5 ℃靜置處理 21
3.2.2 常溫25 ℃靜置處理 21
3.3 結論 22

第四章 結果與討論-貳 24
貳、兩類型SA級魚漿本質差異及凝膠機制研究 24
4.1 兩類型魚漿本質之差異 24
4.1.1 碎肉魚漿 25
4.1.2 加鹽魚漿 26
4.2 兩類型魚漿靜置凝膠機制之探討 27
4.2.1 熱描剛性測定儀 28
（1）低溫5 ℃靜置處理 29
（2）常溫25 ℃靜置處理 29
4.2.2 示差掃描熱分析儀 30
（1）低溫5 ℃靜置處理 31
（2）常溫25 ℃靜置處理 32
4.3 結論 33

第五章 結果與討論-參 34
參、水分及澱粉添加對魚糕成品品質的影響 34
5.1 水分對魚糕成品質感之影響 34
5.1.1 未經靜置與市販品比較 35
5.1.2 有經靜置與市販品比較 36
5.2 不同水分及澱粉添加對魚糕成品質感之影響 36
5.2.1 未經靜置與市販品比較 37
5.2.2 有經靜置與市販品比較 37
5.3 結論 38

第六章 總結 39

參考文獻

何淇義。2000。吳郭魚魚漿之靜置處理條件對魚糕品質的影響。國立臺灣海洋大學食品科學系碩士學位論文。基隆。
周志正。2002。阿拉斯加鱈魚魚漿生產煉製品的擂潰及靜置製程之機制及最適化研究。國立臺灣海洋大學食品科學系碩士學位論文。基隆。
林雅華。1996。青魚死後僵直及嫩化作用對肉品品質影響。國立臺灣海洋大學水產食品科學系碩士學位論文。基隆。
祝永平。1993。以示差掃描熱量分析技術探討淡水吳郭魚魚漿成膠機構。國立臺灣海洋大學水產食品科學研究所碩士學位論文。基隆。
侯奕安。2002。冷凍阿拉斯加鱈魚魚漿所製備魚糕成品質感之評估。國立臺灣海洋大學食品科學系碩士學位論文。基隆。
陳怡伶。1998。吳郭魚、鱈魚及其混合魚漿之靜置促凝膠機制及品質改良。國立臺灣海洋大學水產食品科學系碩士學位論文。基隆。
陳東輝。1995。吳郭魚死後僵直嫩化作用對肉品品質的影響。國立臺灣海洋大學水產食品科學研究所碩士學位論文。基隆。


黃一菁。1993。利用熱分析技術研究肌肉/肉漿之相轉移及魷魚魚漿成膠機制。國立臺灣海洋大學水產食品科學研究所碩士學位論文。基隆。
黃綉娟。1994。肌原纖維蛋白質多重組態之熱分析鑑識。國立臺灣海洋大學水產食品科學研究所碩士學位論文。基隆。
漁業年報。2003。行政院農委會漁業署。
蘇崇文。1996。以DSC、TRM、TSRM研究魚肉及魚糕品質。國立臺灣海洋大學水產食品科學研究所博士學位論文。基隆。
An, H., Peters, M. Y. and Seymour, T. A. 1996. Role of endogenous enzymes in surimi gelation. Trends Food Sci. Technol. 7: 321-326.
A. O. A. C. （Association of Official Analytical Chemists）. 1984. Ed. By Horwitz, W. Official Methods of Analysis. 13th ed. Washington, D. C. USA.
Alvarez, C., Couso, I., and Tejada, M. 1995. Sardine surimi gels as affected by salt concentration, blending, heat treatment and moisture. J. Food Sci. 60: 622-626.
Araki, H., and Seki, N. 1993. Comparison of reactivity of transglutaminase to various fish actomyosin. Bull. Jap. Soc. Fish. 59: 711-716.
Asghar, A., Samejima, K., and Yashi, T., 1985. Functionality of muscle proteins in gelation mechanisms of structured meat products. Crit. Rev. Food Sci. Nutr. 22: 22-27.
Benjakul, B., Visessanguan, W., and Thummaratwasil, P., 2000. Inhibition of gel weakening of threadfin bream surimi using thai legume seed proteinase inhibitors. J. Food Biochem. 24: 363-380.
Benjakul, S., Chantarasuwan, C., Visessanguan, W., 2003. Effect of medium temperature setting on geling characteristics of surimi from some tropical fish. Food Chem. 82: 567-574.
Couso, I., Alvarez, C., Sola, M. T., Barba, C., Tejada, M. 1998. Morphology of starch in surimi gels. Z. Lebensm. Unters. Forsch. A. 206:39-43.
Folk, J. E. 1980. Transglutaminases. Annual Review Biochemistry. 49: 517-531.
Folk, J. E., Cole, P. W. and Mullooly, J. P. 1967. Mechanism of action of guinea pig liver transglutaminase. Ⅱ: The role of metal in enzyme activation. J. Biol. Chem. 242: 1838-1844.
Goll, D. E., Robson, R. M. and Stromer, M. H., 1977. Muscle protein .In “Food protein”, J. R. Whitaker. and S. R. Tannenbaum （Ed.）, AVI Publishing Co, Westport, Connecticut. U. S. A.
Hastings, R. J., Rodger, G. W., Park, R., Matthews, A. D., and Anderson, E. M. 1985. Differential scanning calorimetry of fish muscle: The effect of processing and species variation. J. Food Sci. 50: 503-510.
Ho, M. L., Chen, G. H., and Jiang, S. T. 2000. Effect of mackerel cathepsins L and L-like, and calpain on the degradation of mackerel surimi. Fisheries Sci. 66: 558-568.
Hsu, C. K., and Chiang, B. H. 2002 Effects of water, oil, starch, calcium carbonate and titanium dioxide on the colour and texture of threadfin and hairtail surimi gels. Int. J. Food Sci. Technol. 37:387-393.
Iso, N., Mizuno, H., Ogawa, H., Mochizuki, Y., and Masuda, N. 1991. Differential scanning calorimetry on fish meat paste. Nippon Suisan Gakkaishi 57: 337-340.
Jacob, D. K. and Sebranek, J. G. 1980. Use of prerigor beef for frozen ground beef patties. J. Food Sci. 45: 648-651.
Joseph, D., Lanier, T. C., and Hamann, D. D. 1994. Temperature and pH affect transglutaminase-catalyzed “setting” of crude fish actomyosin. J. Food. Sci. 59:1018-1023.
Kamath, G. G., Lanier, T. C., Foegeding, E. A. and Hamann, D. D. 1992. Nondisulfide covalent cross-linking of myosin heavy chain in “ Setting ” of Alaska pollock and Atlantic croaker surimi. J. Food Biochem. 16: 151-172.
Kijowski, J. M. and Mast, M. G. 1988a. Thermal properties of proteins in chicken broiler tissues. J. Food Sci. 53: 363-366.
Kijowski, J. M. and Mast, M. G. 1988b. Effect of sodium chloride and phosphates on the thermal properties of chicken meat proteins. J. Food Sci. 53: 367-370, 387.
Kimura, I., Sugimoto, M., Toyoda, K., Seki, N., Arai, K. I., and Fujita, T. 1991. A study on cross-linking reaction of myosin in kamaboko " suwari " gels. Nippon Suisan Gakkaishi 57: 1389-1396.
Korhonen, R. W., Lanier, T. C., and Giesbrecht F. 1990. An evaluation of simple method for following rigor development in fish. J. Food Sci. 55: 346-351.
Kuraishi, C., Yamazaki, K., and Susa Y. 2001. Transglutaminase:it’s utilization in the food industry. Food Rev. Int. 17: 221-246
Lee, C. M. 1984. Surimi process technology. Food Technol.38: 69.
Lee, C. M. 1985. A pilot plant study of surimi making properties of Red Hake （Urophycis chuss） in proceeding of the Intl. Sym. on Eng. Seafood Including Surimi, NFI.
Lee, C. M. 1994. Surimi processing from lean fish. In Seafoods: Chemistry, Processing Technology and Quality, F. Shahidi and J. R. Botta （Ed.）, （pp. 263-287）. Blackie Academic and Professional, London.
Lefevre, F., Fauconneau, B., Ouali, A., and Culioli, J. 1998. Thermal gelation of brown trout myofibrils: effect of muscle type, heating rate and protein concentration. J. Food. Sci. 63: 299-304.
Lo, J. R., Mochizuki, Y., Nagashima, Y., Tanaka, M., Iso, N., and Taguchi, T. 1991. Thermal transitions of myosins / subfragments from black marlin （Makaira mazara） ordinary and dark muscles. J. Food Sci. 56: 954-957.
Lowey, S., Slayter, H. S., Weed, A. G. and Baker, H. 1969. Substructure of the myosin moleule I. Subfragments of myosin by enzymic degradation J. Mol. Biol.42: 1-29.
Ma, L. B., Yamanaka, H., Ushio, H., and Watabe, S. 1992. Studies on the mechanism of thaw rigor in Carp. Nippon Suisan Gakkaishi 58: 1535-1540.
Matsuura, M. and Arai K-I. 1987. Effect of rabbit light-meromyosin on filament forming ability of fish myosin and biochemical properties of their co-filament. Nippon Suisan Gakkaishi 53: 109-118.
Montejano, J. G., Hamann, D. D., and Lanier, T. C. 1983. Final strengths and rheological changes during processing of thermally induced fish muscle gel. J. Rheology 27: 557-565.
Montejano, J. G., Hamann, D. D. and Lanier, T. C. 1984. Thermally induced gelation of selected comminuted muscle systems－Rheological changes during processing , final strengths and microstructure. J. Food Sci. 49: 1496-1505.
Mori, K., Ojima, T. and Kiyoyoshi, K. 1989. Comparative studies on ATPase activity and filament assembly of akazara and vertebtate myosins. Nippon Suisan Gakkaishi 55: 1851-1856.
Morrissey, M. T. and Tan, S. M. 2000. World resources for surimi. In J. W. Park （Ed）, surimi and surimi seafood （pp. 1-22）. Marcel Dekker, Inc, New York.
Niwa, E. 1975. Role of hydrophobic bonding in gelation of fish flesh paste. Bull. Jap. Soc. Sci. Fish. 41: 907-910.
Niwa, E. 1992. Chemistry of surimi gelation. In “ Surimi Technology ”, T. C. Lanier. and C. M. Lee （Ed.）, pp. 389-427. Marcel Dekker, Inc., New York.
Niwa, E., Inuzuka, K., Nowsad, A., Dajia, L. and Kanoh, S. 1995. Contribution of SS bond to the elasticity of actomyosin gel in which coexisting transglutaminase was inactivated. Fisheries Sci. 61: 438-440.
Niwa, E., Sato, K., Suzuki, R., Nakayama, T., and Hamada, I. 1981. Fluorometric study of setting properties of fish flesh sol. Bull. Jap. Soc. Sci. Fish. 47: 817-821.
Niwa, E., Nowsad, A. A., and Kanoh, S. 1991. Comparative studies on the physical parameters of kamabokos treated with the low temperature setting and high temperature setting. Nippon Suisan Gakkaishi 57: 105-109.
Noguchi, S. F. 1986. Dynamic viscoelastic changes of surimi （minced fish meat） during thermal gelation. Bull. Japan. Soc. Sci. Fish. 52: 1261-1274.
Nowsad, A. AKM., Kanoh, S., and Niwa, E. 1996. Contribution of transglutaminase to the setting of fish pastes at various temperatures. Fisheries Sci. 62: 197-204.
Obinata, T., Maruyama, K., Sugita, H., Kohama, K., and Edashi, S. 1981. Dynamic effects of structural proteins in vertebrate skeletal muscle. Muscle Nerve. 4: 456-461.
Park, J. W. and Lanier, T. C. 1987. Combined effects of phosphates and a sugar or polyol on protein stabilization fo fish myofibrils. J. Food Sci. 52: 1509-1521.
Park, J. W. and Lanier, T. C. 1989. Scanning calorimetric behavior of tilapia myosin and actin due to processing of muscle and protein purification. J. Food Sci. 54: 49-51.
Park, J. W., Lanier, T. C., and Pilkington, D. H. 1993. Cryostabilization of functional properties of pre-rigor and post-rigor beef by dextrose polymer and/or phosphates. J. Food Sci. 58: 467-472.
Pearson, A. M. and Young, R. B. 1990. Muscle and Meat Biochemistry. A. M. Pearson. And R. B. Young （Ed.）, pp. 66-129. Academic Press. New York.
Quinn, J. R., Raymond, D. P., and Harwalkar, V. R. 1980. Differential scanning calorimetry of meat proteins as affected by processing treatment. J. Food Sci. 45: 1146-1449.
Ragshaw, C. R. 1993. Contractile preteins. In Muscle Contraction, C. R. Ragshaw （Ed.）, （pp. 33-55）. Chapman ＆ Hall, London.
Samejima, K., Ishioroshi, M. and Yasui, T. 1981. Relative roles of the head and tail portions of the molecule in heat-induced gelation of myosin. J. Food Sci. 26: 1412-1418.
Samejima, K., Ishioroshi, M. and Yasui, T. 1983. Scanning calorimetric studies on thermal denaturation of myosin and its subfragments. Agric. Boil. Chem. 47: 2373-2380.
Sano, T., Noguchi, S. F., Matsumoto, J. J. and Tsuchiya, T. 1990. Thermal gelation characteristics of myosin subfragment. J. Food Sci. 55: 55-58, 70.
Sato, S., Akagawa, N., Tsuchiya, T., and Matumoto, J.J. 1987. Electron microscopic study on the processes of preparation of kamaboko. Nippon Suisan Gakkaishi 53: 649-658.
Sato, S., Nakagawa, N., Terui, S., Tsuchiya, T. 1990a. Effects of polyphosphates in dispersion state of protein in Alaska pollack frozen surimi. Nippon Suisan Gakkaishi 56: 1299-1306.
Sato, S., Nakagawa, N., Terui, S., Tsuchiya, T. 1990b. Effects of pyrophosphates and divalent metal ions（Mg2+，Ca2+）on carp actomyosin. Nippon Suisan Gakkaishi 56: 1655-1660.
Schmidt, G. R., Cassens, R. G., and Briskey, E. J. 1968. Development of an isotonic-isometric rigor meter. J. Food Sci. 33: 239.
Seymour, T. A., Morrissey, M. T., Peters, M. Y. and Haejung, A. 1994. Purification and characterization of Pacific whiting proteases. J. Agric. Food Chem. 42: 2421-2427.
Stabursvik, E. and Martens, H. 1980. Thermal denaturation of proteins in post rigor muscle tissue as studied by differential scanning calorimetry. J. Sci. Food Agric. 31: 1034-1042.
Suzuki, T. 1981. Characteristics of fish meat and fish protein. In Fish and Krill Protein. T. Suzuki （Ed.）, （pp. 1-56）. Applied Science Publishers Ltd, London.
Sych, J., Lacroix, C., Adambounou, L. T., and Castaigen, F. 1990a. Cryoprotectve effects of lactitol, palatinit and polydextrose on cod surimi proteins during frozen storage. J. Food Sci. 55: 356-360.
Sych, J., Lacroix, C., Adambounou, L. T., and Castaigen, F. 1990b. Cryoprotectve effects of some materials on cod- surimi proteins during forzen storage. J. Food Sci. 55: 1222-1227, 1263.
Thorarinsdottir, K. A., Arason, S., Geirsdottir, M., Bogason S.G., Kristbergsson, K. 2002. Changes in myofibrillar proteins during processing of salted cod (Gadus morhua) as determined by electrophoresis and differential scanning calorimetry. Food Chem. 77: 377-385.
Tsuchiya, T., Yamada, N. and Matsumoto, J. J. 1978. Physico-chemical properties of squid myosin. Bull. Jap. Soc. Sci. Fish. 44: 181-184.
Wan, J., Kimura, I. And Seki, N. 1995. Inhibitory factors of transglutaminase in salted salmon meat paste. Fisheries Sci. 61: 968-972.
Wu, M. C., Akahane, T., Lanier, T. C. and Hamann, D. D. 1985a. Thermal transitions of actomyosin and surimi prepared from Atlantic croaker as studied by differential scanning calorimetry. J. Food Sci. 50: 10-13.
Wu, M. C., Akahane, T., Lanier, T. C., and Hamann, D. D. 1985b. Rigidity and viscosity changes of croaker actomyosin during thermal gelation. J. Food Sci. 50: 14-19.
Wright, D. J., Leach, I. B. and Wilding, P. 1977. Differential scanning calorimetric studies of muscle and its constituent protein. J. Sci. Food Agric. 28: 557-564.
Yang, H., and Park, J. W. 1998. Effects of starch properties and thermal-processing conditions on surimi-starch gels. Lebensm.-Wiss. U.-Technol. 31:344-353.
Yasueda, H., Kumazawa, Y., Motoki, M. 1994. Purification and characterization of a tissue-type transglutaminase from red sea bream （pagrus major）. Biosci. Biotechnol. Biochem. 58: 2041-2045.
Yasui, T., Ishioroshi, M., and Samejima, K. 1980. Heated-induced gelation of myosin in the presence of actin. J. Food Biochem. 4: 61-78.
Yasui, T., Ishioroshi, M., and Samejima, K. 1982. Effect actomyosin on heat-induced gelation of myosin. Agric. Biol. Chem. 46: 1049-1059.
Yokomoto, K. and Nishita, K. 1989. Earliest event in heat-denaturation of Akazara myosin. Nippon Suisan Gakkaishi. 53: 159-164.
Yongsawatdigul, J., Worratao, A., and Park, J. W. 2002. Effect of endogenous transglutaminase on threadfin bream surimi gelation. J. food sci. 67: 3258-3263.