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研究生:林后儀
研究生(外文):Hou-Yi Lin
論文名稱:凍結貯藏對鋸峰齒鮫肌肉蛋白之影響
論文名稱(外文):Effect of Forzen Storage on the Muscle Protein of Prionace glauca
指導教授:曹欽玉
學位類別:碩士
校院名稱:國立海洋大學
系所名稱:食品科學系
學門:農業科學學門
學類:食品科學類
論文種類:學術論文
論文出版年:2002
畢業學年度:90
語文別:中文
論文頁數:74
中文關鍵詞:凍結貯藏鋸峰齒鮫魚漿肌肉蛋白
外文關鍵詞:frozen storageprionace glaucasurimimuscle protein
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摘要
冷凍鋸峰齒鮫(Prionace glauca,俗稱水鯊魚)在魚糕的製造過程中,面臨形膠能力不佳的問題,以其為原料所做出來之煉製品品質甚差。因此本研究主要在探討凍結及凍藏條件對鋸峰齒鮫魚肉蛋白質性質之影響,以期改善其凝膠性質及提高鋸峰齒鮫煉製品的品質。將原料魚肉片(15㎝×5㎝×1㎝)分別以靜置式(-20℃)及送風式(-37℃)兩種方式凍結後,置於-20℃凍藏四個月,觀察其凍藏期間魚肉肌動凝蛋白抽出量、鈣核苷三磷酸酶比活性、總硫氫基及可反應硫氫基之含量變化,並製成魚糕做品質測定。結果顯示此兩種不同凍結方式之肌動凝蛋白抽出量、鈣核苷三磷酸酶比活性、總硫氫基及可反應硫氫基之含量變化,均隨貯藏時間之增加而下降,但其後隨貯藏時間之延長,-37℃凍結組下降的速率較-20℃組緩和。測定此凍藏期間之魚肉所製成魚糕的膠強度,在凍藏第六週時,-37℃凍結組之變化由478 g×㎝下降至307 g×㎝,而-20℃組則由422 g×㎝下降至228 g×㎝,後者的膠強度比前者較差。
將魚肉片以-37℃凍結後,分別放置在恆定溫度-20℃、-40℃與變動溫度(每週在-20℃三天、在-40℃四天)下凍藏四個月,以探討凍藏條件對鋸峰齒鮫肌肉蛋白質及魚糕品質之影響。結果顯示在-40℃恆定溫度下凍藏的變化比其他兩組較為緩慢,在魚糕的膠強度方面,凍藏第十二週仍有351 g×㎝為最佳。
原料魚經採肉、除筋、脫水後,添加0.3%重合磷酸鹽與抗凍劑(8%蔗糖或4%蔗糖+4%山梨糖醇)製成冷凍魚漿,分別置於-20℃及-40℃凍藏,觀察其肌肉蛋白質及魚糕品質之變化。結果顯示不論在-20℃或-40℃凍藏三個月,添加抗凍劑之二組其肌動凝蛋白抽出量、鈣核苷三磷酸酶比活性、總硫氫基及可反應硫氫基之含量變化,均比未添加抗凍劑組佳,下降趨勢較為緩和,且仍然保有良好的魚糕品質。

Abstract
Owing to the frozen blue shark (Prionace glauca) meat was found difficultly to form network of meat sol and make a good quality of kamaboko. Therefore, to understand muscle protein properties and improve the gel-forming ability of blue shark, the fillets and minced meat products, adding 0.3% polyphosphates and 8% sucrose or 4% sucrose and sorbitol as cryoprotectants, were freezing with still freezer (-20oC) and air-blaster freezer (-37oC), respectively. All samples were stored at —20oC, —40oC and/or fluctuated temperature (—20oC, 3 days; —40oC 4 days), respectively; and then took out for thawing and detecting the extractable actomyosin, Ca++-ATPase specific activity, reactive and total —SH group; and using SDS-polyacrylamide gel electrophoresis to analyze the changes of myofibrillar protein; and making into kamaboko in an interval period. The quality of kamaboko was also monitored with breaking force, deformation, water-holding capacity and color.
From the results, the extractable actomyosin, Ca++-ATPase specific activity, reactive and total —SH groups and the quality of kamaboko produced from frozen fillet were found that the two freezing conditions had the same decline and sharply decreasing with the extending storage time and no significant difference between each other. As for the effect of frozen storage condition, the gel-forming ability and the quality of kamaboko made from —40oC group fillet was found better than that of the other two groups. Either —20oC or —40oC frozen storage minced meat products, it was found remarkably to improve the gel-forming ability and the quality of kamaboko which with or without cryoprotectants at initial state; and the former was better than that of the later during frozen storage 3 months.

目 錄
頁數
中文摘要……………………………….….……………………… 1
英文摘要…………………………………………………………… 2
壹、前言…………………………………………………………. 3
貳、文獻整理……………………………………………………… 5
一、鯊魚肉之性質………………………………………………. 5
(一)鯊魚肉之一般組成分………………………………… 5
(二)鯊魚肉蛋白質之組成………………………………… 5
二、魚肉蛋白質之組成.………………………………………… 6
(一)肌漿蛋白質…………………………………………… 6
(二)基質蛋白質…………………………………………… 6
(三)肌纖維蛋白質………………………………………… 7
三、凍藏引起之蛋白質變性.…………………………………… 9
(一)凍藏中魚肉蛋白質凝聚之機制……………………… 9
1.蛋白質分子之凝聚……………………………………. 9
2.蛋白質分子構形之展開………………………………. 10
(二)造成冷凍變性之原因………………………………… 10
1.脫水……………………………………………………. 10
2.分子間架橋之形成……………………………………. 10
3.凍結速率、凍藏溫度及時間對魚肉蛋白質之影響…. 11
3.1.凍結速率……….….……………………………….. 11
3.2.凍藏溫度與時間………..………………………….. 12
四、魚漿的形膠作用………………..…………………………… 12
五、魚漿的解膠作用..…………………………………………… 13
六、影響魚漿形膠之因素…..…………………………………… 14
(一)魚種……….…………………………………………… 14
(二)形膠溫度與時間…….………………………………… 15
(三)pH值…………………….…………………………….. 16
(四)添加還原劑………………….………………………… 16
(五)魚肉蛋白酶…….……………………………………… 17
(六)蛋白酶抑制劑…………….…………………………… 17
七、抗凍劑……………………………………………………….. 18
(一)磷酸鹽類……………….……………………………… 18
(二)有機化合物……………….…………………………… 19
(三)冷凍變性抑制劑之作用機制….……………………… 20
參、實驗材料與方法……………………………………………… 22
一、實驗材料….…………………………………………………. 22
二、試藥…….……………………………………………………. 22
三、儀器…….……………………………………………………. 22
四、實驗步驟與方法…………………….………………………. 23
(一)冷凍鋸峰齒鮫魚肉片之製備..………………………... 23
(二)鋸峰齒鮫冷凍魚漿之製備….………………………… 23
(三)水分測定….…………………………………………… 23
(四)可壓出水分之測定…….……………….……………... 23
(五)肌動凝蛋白之抽出……………………………………. 24
(六)肌動凝蛋白濃度之測定………………………………. 24
(七)肌動凝蛋白Ca++-ATPase活性之測定……………….. 24
(八)肌動凝蛋白總硫氫基與可反應硫氫基含量之測定…. 25
(九)電泳分析………..……………………………………...…26
(十)魚糕品質之測定………………..…………………...……26
1.魚糕之製備…………………….………………………. 26
2.凝膠強度之測定..……………………………………… 26
3.曲折試驗……………………..………………………… 27
4.色澤之測定……….…………………………………… 27
(十一)統計分析………………………………………………. 27
肆、結果與討論………………………………………….. 28
一、凍結條件對鋸峰齒鮫魚肉蛋白性質之影響…………….. 28
1.鋸峰齒鮫魚肉之凍結速率………………………….… 28
2.鋸峰齒鮫魚肉可壓出水分之變化………………….… 28
3.肌動凝蛋白抽出量之變化………………………….… 29
4.肌動凝蛋白可反應硫氫基與總硫氫基之變化…….… 29
5.鈣核苷三磷酸酶比活性之變化………………………. 31
6.魚糕製品成膠能力之變化……………………………. 31
二、凍藏條件對鋸峰齒鮫魚肉蛋白性質之影響…………….. 32
1.鋸峰齒鮫魚肉可壓出水分之變化……………………. 32
2.肌動凝蛋白抽出量之變化……………………………. 32
3.肌動凝蛋白可反應硫氫基與總硫氫基之變化………. 33
4.鈣核苷三磷酸酶比活性之變化…………………….… 33
5.魚糕製品成膠能力之變化……………………………. 34
三、抗凍劑對鋸峰齒鮫魚漿凍藏期間品質之影響………… 34
1.鋸峰齒鮫魚漿可壓出水分之變化….………………… 34
2.肌動凝蛋白抽出量之變化……………………………. 34
3.肌動凝蛋白可反應硫氫基與總硫氫基之變化………. 35
4.鈣核苷三磷酸酶比活性之變化………………………. 35
5.魚糕製品成膠能力之變化……………………………. 36
6.魚糕製品之色澤…….………………………………… 36
伍、結論………………………………………………… 37
陸、參考文獻……………………………………………………. 38
圖……………………………………………………….……. 51
表……………………………………………………….……. 71

陸、參考文獻
于名振,1986,台灣脊椎動物誌,pp.69,台灣商務印書館發行。
吳清熊,1987,魚肉蛋白質,pp.63,華香園出版社,台北。
吳清熊,1991,台灣水產加工業現況,pp.88,台灣省漁業局發行。
李佳芸,1999,由Escherichia coli 生產sulfite reductase,國立台灣海洋大學食品科學研究所碩士論文,基隆。
孫寶年、李國皓、翁秀貞,1986,台灣地區常見食用魚貝類圖說,pp75,行政院衛生署編印。
鄭森雄,1977,台灣水產加工業實況,pp.118,農業復興委員會發行。
藍群傑,孫寶年,江善宗,1987,還原劑對冷凍狗母魚魚漿蛋白質變性及煉製品成膠之影響,中國農業化學會誌,25(2):159-168。
田中武夫,1973,魚肉凍結に伴ウ水の舉動,”食品の水”,pp.63-82,恆星社厚生閣,東京,日本。
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、鴻巢章二,1987a,水產食品學,pp.21-37,恆星社厚生閣,東京,日本。
須山三千三、鴻巢章二,1987b,水產食品學,pp.48,恆星社厚生閣,東京,日本。
關伸夫,1977,魚類筋原纖維質,”魚肉蛋白質”,pp.7-23,恆星社厚生閣,東京,日本。
Akahane,Y. and Shimizu, Y. 1989. Effect of pH and sodium chloride on the water holding capacity of surimi and its gel. Nippon Suisan Gakkaishi. 55:1827.
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.
AOAC. 1984. Official Methods of Analysis, 14th ed. Association of Official Analytical Chemists: Washington, D.C.
Arai, K. 1974. Evaluation of fish quality from the muscle protein studies. In “Quality of Fish”, pp.55-80, ed. by Jap. Soc. Sci. Fish. Koseisha, Tokyo.
Arai, K. and Fukuda, M. 1973. Studies on muscular proteins of fish XII. Effect of temperature on denaturation of actomyosin ATPase from carp muscle. Nippon Suisan Gakkaishi. 39:625-631.
Arai, 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.
Arakawa, T. and Timasheff S. N. 1982. Stabilization of protein structure by sugar. Biochemistry. 21:6536-6544.
Araki, H. and Seki, N. 1993. Comparison of reactivity of transglutaminase to various fish actomyosins. Bull. Jap. Soc. Sci. Fish. 59:711-716.
Asghar, A. and Yeates, N. T. 1986. Functionality of muscle protein in gelation mechanisms of structured meat products. CRC. crit. Rev. Food Sci. Nutri. 10:115.
Asghar, A., Samejima, K and Yasui, T. 1984. Functionality of muscle protein in gelation mechanisms of structured meat products. CRC. crit. Rev. Food Sci. Nutri. 22(1):27-106.
Aspinwall, N. and Tsuyuki, H. 1963. Inheritance of muscle proteins in hybrids between the red shiner (Richardsonius balteatus) and the peamouth chub (Mylocheilus carurinum). J. Fish. Bd. Canada 25:1317.
Bevilacqua, A. E. and Zarttzky, N. E. 1980. Ice morphology in frozen beef. J. Food Technol. 15:589.
Bevilacqua, A. E., Zarttzky, N. E. and Calvelo, A. 1979. Histological measurements of ice in frozen beef. J. Food Technol. 14:237.
Boye, S. W. and Lanier, T. C. 1988. Effects of heat stable alkalilne protease activity of atlantic menhaden (Brevoorti tyrannus) on surimi gels. J. Food Sci. 53: 1340-1398.
Burgarella, J. C., Lanier, T. C. and Hamann, D. D. 1985a. Effects of added egg white or whey protein concentrate on thermal transitions in rigidity of croaker surimi. J. Food Sci. 50:1588-1594.
Burgarella, J. C., Lanier, T. C., Hamann, D. D. and Wu, M. C. 1985b. Gel strength development during heating of surimi in combination with egg white or whey protein concentrate. J. Food Sci. 50:1595-1597.
Buttkus, H. 1970. Accelerated denaturation of myosin in frozen solution. J. Food Sci. 35:558-562.
Buttkus, H. 1971. The sulfhydryl content of rabbit and trout myosins in relation to protein stability. Can. J. Biochem. 49:97-101.
Chang, C. C. and Regenstein J. M. 1997. Textural changes and functional properties of cod mince proteins as affected by kidney tissue and cryoprotectants. J. Food Sci. 62:299-304.
Chang-Lee, M. V., Lampila, L. E. and Crawford. D. L. 1990. Yield and composition of surimi from Pacific whiting (Merluccius productus) and the effect of various protein additives on gel strength. J. Food Sci. 55:83-86.
Chang-Lee, M. V., Pacheco-Aguilar, R., Crawford. D. L. and Lampila, L. E. 1989. Proteolytic activity of surimi from Pacific whiting (Merluccius productus) and heat-set gel texture. J. Food Sci. 54:1116-1119.
Chen, C. S., Hwang, D. C. and Jiang, S. T. 1988. Purification and characterization of milk fish (Chanos chanos) myosin. Nippon Suisan Gakkaishi. 54:1423-1427.
Chen, C. S., Hwang, D. C. and Jiang, S. T. 1989. Effect of storage temperatures on the formation of disulfides and denaturation of milkfish myosin (Chanos chanos). J. Agric. Food Chem. 37:1228-1232.
Cheng, C. S., Hamann, D. D. and Webb, N. B. 1979. Effect of thermal processing on minced fish gel texture. J. Food Sci. 44:1080-1086.
Chrystall, B. B.1972. Influence of storage temperatures on quality of meat. Meat Industry Research Institute of New Zealand (INC) 274:1.
Colmenero, F. J. and Borderius, A. J. 1983. A study of the effects of frozen on certain functional properties of meat and fish protein. J. Food. Technol. 18:731.
Connell, J. J. 1959. Aggregation of cod myosin during frozen storage. Nature. 183:664-668.
Connell, J.J. 1960. Changes in the adenosine triphosphatase acitivity and sulfhydryl group of cod flesh during frozen strotage. J. Sci. Food Agric. 11:245.
Ellinger, R. H. 1976. Phosphate as food ingredients. pp.4-11, Academic Press. New York.
Franks, F. 1975. Water, ice and solutions of simple molecules. In “Water Relstion of Foods”, pp.3-22, ed. by Duckworth, R. B. Academic Press, London.
Fukuda, Y. 1986. Effect of freezing condition on quality of frozen fish meat. Refrigeration (Japan). 61:18.
Fukuda, Y., Tarakita, Z. and Arai, K. 1984. Effect of freshness of chub mackerel on the freeze-denatruation. Bull. Jap. Soc. Sci. Fish. 50:845-852.
Fukuda, Y., Tarakita, Z., Kawamura, M., Kakehata, K. and Arai, K. 1982. Denatruation of myofibrillar protein in chub mackerel. Bull. Jap. Soc. Sci. Fish. 48:1672-1632.
Fukuda, Y., Yamaguchi, T., Sakukida, Y. and Kawamura, K. 1981. Effect of pH on the freezing denaturation of mackerel myofibrillar proteins. Meeting of All-Japan Fishery Research Stations on Marine Products (Fisheries Agency). pp.81-84.
Funastsu, Y. and Arai, K. 1991. The pH-dependence of changes in gel forming ability and myosin heavy chain of salt-ground meat from walleye pollack. Nippon Suisan Gakkaishi. 57:1973.
Funastsu, Y., Kato, N. and Arai, K. 1993. Gel forming ability and cross-linking ability of myosin heavy chain of salt-ground meat from sardine surimi acidified by lactic acid. Nippon Suisan Gakkaishi. 59:1093-1098.
Goldblith., S. A. 1969. The problems of storage of lyophilized food products. In “Recent Developments in Freeze-dring”, Vol. II. Surface reactions in Freeze-dried systems, IIR Commission X, Paris. 9:41.
Goldblith., S. A. and karel, M. 1966. Stability of freeze-dried food. In “Advanced in Freeze-dring” Rey, L., ed. Hermann, Paris. pp.191- 225.
Goll, D. E., Robson, R. M. and Stromer, M. H. 1977. Muscle proteins. In “Food Protein” pp.121-123 ed. by John R. Whitaker and Steven R. Tannenbaum, Pub. by AVI, U.S.A.
Groninger, H., Hawkes, J. W. and Babbitt, J. K. 1983. Function and morphological changes in processed frozen fish muscle. J. Food Sci. 48:1388.
Haard, N. F. 1990. Enzymes from food myosystems. J. Muscle Foods 1:292.
Haard, N. F. 1992. A review of proteolytic enzymes from marine organisms and their application in the food industry. J. Aquatic Food Product Tech.1:17-35.
Hamada, I., Tsuji K., Nakayama, T. and Niwa, E. 1977. Oxidative denaturation of actomyosin. Bull. Jap. Soc. Sci. Fish. 43:1105.
Hamann, D. D., Amato, P. M., Wu, M. C. and Foegeding, E. A. 1990. Inhibition of modori (gel weakening) in surimi by plasma hydrolysate and egg white. J. Food Sci. 55:665-669.
Hashimoto, A. and Arai, K. 1978. The effect of pH and temperature on the stability of myoflbrillar Ca-ATPase from some fish species. Nippon Suisan Gakkaishi. 44:1389.1393.
Hofmann, K. and Hamm, R. 1978. Sulfhydryl and disulfide groups in meats. Adv. Food Res. 24:2.
Hsu, C. K., Kolbe, E., Morrissey, M. T. and Chung, Y. C. 1993. Protein denaturation of frozen Pacific whiting (Merluccius productus) fillets J. Food Sci. 58:1055-1056,1075.
Huber, C. S., Harrington, R. B. and Staelman, W. J. 1970. Effect of freezing rate and freeze drying on the soluble proteins of muscle. J. Food. Sci. 35:233.
IIR (Intern. Inst. Refrign) 1972. Recommendations for the processing and handling of frozen foods. 2nd. Paris.
Ishida, M., Sugiyama, N., Sato, M. and Nagayama, F. 1995. Two kinds of neutral serine proteinases in salted muscle of anchovy, Engraulis japonica. Biosci. Biotech. Biochem. 59:1107.
Ishioroshi, M., Samejima, K. and Yasui, T. 1979. Heat-induced gelation of myosin: factors of pH and salt concentrations. J. Food Sci. 44:1280-1284.
Ito, M. Inoue, N. and Shinano, H. 1990. The effect of freezing time on the freeze denaturation of carp myosin. Nippon Suisan Gakkaishi. 56:307.
Ito, M. Inoue, N. and Shinano, H. 1991. Denaturation of carp myosin B during slow freezing. Nippon Suisan Gakkaishi. 57:319.
Itoh, Y., Sompongse, W. and Obatake, A. 1996. Effect of cryoprotectants and a reducing reagent on stability of actomyosin during ice storage. Fisheries Sci. 62:73-79.
Itoh, Y., Yoshinaka, R. and Ikeda, S. 1979. Effects of inorganic reducing agents on the gel formation of fish meat by heating. Bull. Japan. Soc. Sci. Fish. 45:455-461.
Itzhaki, R. F. and Gill, D. M. 1964. A micro-biuret method for estimating proteins. Anal. Biochem. 9:401.
Iwata, K., Kobashi, K. and Hase, J. 1974a. Some enzymatic properties of carp muscular alkaline protease. Nippon Suisan Gakkaishi. 40:189-200.
Iwata, K., Kobashi, K. and Hase, J. 1974b. Effect of carp muscular alkaline protease upon modori phenomenon in kamaboko production. Nippon Suisan Gakkaishi. 40:1051-1058.
Jiang, S. T. 1977. Studies on the denaturation of mullet muscle protein during frozen storage. Refrigeration (Japan). 52:621.
Jiang, S. T. and Lee, T. C. 1985. Changes in free amino acid and protein denaturation of fish muscle during frozen storage. J. Agric. Food Chem. 33:839.
Jiang, S. T., Chu, T. Y., Lan, C. C. and Lee, T. C. 1984. New approach to improve the quality of minced fish products using freeze-thawed cuttlefish. Proceedings of Chinese-American Academic and Professional Convention, Los Angeles, CA, June 29-July 3, Session 3.3, pp.1-5.
Jiang, S. T., Tsao, C. Y. and Lee, T. C. 1987a. Effect of free amino acids on the denaturation of mackerel myofibrillar proteins in vitro during frozen storage. J. Agric. Food Chem. 35:28-33.
Jiang, S. T., Hwang, B. S. and Tsao, C. Y. 1987b. Protein denaturation and changes in nucleotides of fish muscle during frozen storage. J. Agric. Food Chem. 35:22-27.
Jiang, S. T., Hwang, B. S. and Tsao, C. Y. 1987c. Effect of adenosine-nucleotides and their derivatives on the deanturation of myofibrillar proteins in vitro during frozen storage at -20℃. J. Food Sci. 52:117-123.
Jiang, S. T., Hwang, D. C. and Chen, C. S. 1988a. Denaturation and change in SH-group of actomyosin from milkfish during storage at -20℃. J. Agric. Food Chem. 36: 433-437.
Jiang, S. T., Hwang, D. C. and Chen, C. S. 1988b. Effect of storage temperatures on the formation of disulfides and denaturation of milkfish actomyosin (Chanos chanos). J. Food Sci. 53:1333-1335.
Jiang, S. T., Lan, C. C. and Tsao, C. Y. 1986. New approach to improve the quality of minced fish products from freeze-thawed cod and mackeral. J. Food Sci. 51:310-312.
Jiang, S. T., Lee, B. L., Tsao, C. Y. and Lee, J. J. 1997. Mackerel cathepsins B and L effects on thermal degradation of surimi. J. Food Sci. 62:310-315.
Jiang, S. T., San, P. C. and Japit, L. S. 1989. Effect of storage temperatures on the formation of disulfides and denatruation of tilapia hybrid actomyosin. J. Agric. Food Chem. 37(5):1228-1231.
Johnston, D. E., Knight, M. K. and Ledward, D. A. 1992. The chemistry of muscle-based foods. The Royal Society of Chemistry. p.214-222.
Kamath, G. G., Lanier, T. C., Foegeding, E. A. and Hamann, D. D. 1992. Non-disulfide covalent cross-linking of myosin heavy chain in “setting” of Alaska pollock and Atlantic croaker surimi. J. Food Biochem. 16:151-172.
Kanon, S.,Watabe, S. and Hashimoto, K. 1983. Isolation and some physicochemical properties of requiem shark mysion. Bull. Jap. Soc. Sci. Fish. 49(5):757-763.
Kawashima, T., Arai, K. and Saito, T. 1973. Stuides on muscular 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-forming properties of surimi from two species. J. Food Sci. 51:951-956.
Kinoshita, M., Toyohara, H., Shimizu, Y. and Sakaguchi, M. 1992. Modori-inducing proteinase active at 50℃ in threadfin bream muscle. Nippon Suisan Gakkaishi. 58:715-720.
Kirschke, H., Kembhavi, A. A., Bohley, P. and Barrett, A. J. 1982. Action of rat liver cathepsin L on collagen and other substrates. Biochem. J. 201:367-372.
Koreeda, N., Ishigami, T. and Fujita, K. 1982. Kamaboko-forming capacity of shark meat. Bull. Jap. Soc. Sci. Fish. 48(12):1815-1819.
Lanier, T. C. 1986. Functional properties of surimi. Food Technol. 40:573-576,589.
Lanier, T. C. 1988. Muscle protein functional 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. pp.247.
Lee, C. M. 1984. Surimi process technology. Food Technol. 38:69-80.
Levitt, M. and Chothia, C. 1976. Structural patterns in globular protein. Nature. 261:552.
Linko, R. R. and Nikkila, O. E. 1961. Inhibition of the denaturation by salt of myosin in Baltic herring. J. Food Sci. 20:606.
Lowey, S., Slayter, H. S., Weeds, A. G. and Baker, H. 1969. Substruture of the myosin molecule-I. Subfragments of myosin by enzymic degradation. J. Mol. Bol. 42:1.
Makinodan, Y. and Ikeda, S. 1971. Relation between himodori of kamaboko and muscle proteinase. Nippon Suisan Gakkaishi. 37:518-523.
Makinodan, Y., Toyohara, H. and Niwa, E. 1985. Implication of muscle alkaline protease in the textural degradation of fish meat gel. J. Food Sci. 50:1351-1355.
Makinodan, Y., Yamamoto, M. and Simidu, W. 1963. Protease in fish. Nippon Suisan Gakkaishi. 29:776-780.
Mannherz, H. G. and Goody, R. S. 1976. Proteins of contractile systems. Ann. Rev. Biochem. 45:427.
Martino, M. N. and Zarttzky, N. E. 1988. Ice crystal size medications during frozen beef storage. J. Food Sci. 53:1631.
Mason, R. W., Taylor, M. A. J. and Etherington D. J. 1984. The purification and properties of cathipsin L from rabbit liver. Biochem. J. 217:209-217.
Matsukura, U., Okitani, A., Nishimuro, T. and Kato, H. 1981. Mode of degradation of myofibrillar proteins by and endogenous protease, cathepsin L. Biochem. Biophys. Acta. 662:41-47.
Matsumoto, I. and Arai, K. 1987. Influence of concentration ratio of myofibrillar protein and additive like as sorbitol on the freeze denaturation of myofibrils.
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.
Matsumoto, J. J. 1979. Denaturation of fish muscle proteins during frozen storage. In “Protein at Low Temperature” pp.205-224, ed. by Fennma, O., ACS Sympo. Series 180, ACS Washington D.C.
Matsumoto, J. J. 1980. Chemical deterioration of muscle proteins during frozen storage. In “Chemical Deterioration of Proteins”. ACS Sympo. Series. 123. ed. by Whitaker, J. R. and Fujimaki, M. American Chemical Society. Washington, D.C. pp.95-124.
Matsumoto, J. J. and Noguchi, S. 1971. Proc. Int. Congr. Refrig. 13th. Vol.3:237 cited by Matsumoto, J. J. (1980).
Mikami, M., Whiting, A. H., Taylor, M. A. J., Maciewicz, R. A. and Etherington D. J. 1987. Degradation of myofibrils from rabbit, chicken and beef by cathepsin L and lysosomal lysates. Meat Science. 21:81-97.
Miller, R. and Spinelli, J. 1982. The effect of protease inhibitors on proteolysis in parasitized Pacific whiting (Merluccius productus) muscle. Fish. Bull. U. S. 80: 281-286.
Morioka, K. and Shimizu, P. 1990. Contribution of sarcoplasmic protein to gel formation of fish meat. Nippon Suisan Gakkaishi. 53:1073.
Mornet, D., Bonet, A., Audemard, E. and Bonicel, J. 1989. Functional sequences of the myosin head. J. Musc. Cell Motility. 10:10-24.
Morrissey, M. T., Wu, J. W. Lin, D. and An, H. 1993. Protease inhibitor effects on torsion measurements and autolysis of Pacific whiting surimi. Nippon Suisan Gakkaishi. 58:1050-1053.
Murozuka, T. and Arai, K. 1976. Purification and thermostability of myosin Ca-ATPase from the frozen muscle of yellowfin tuna. Bull. Jap. Soc. Sci. Fish. 42:65.
Nagahisa, E., Nishimuro, S. and Fujita, T. 1981. Kamaboko-forming ability of the jellied meat of Pacific hake muscle. Nippon Suisan Gakkaishi. 49:901-906.
Nakai, S. and Lin-chan, E. 1988. Hydrophobic interaction in food systems. CRC press, Inc. Boca Raton. pp.63-128.
Neuhoff, V., Arold, N., Taube, C. and Ehrhardt, W. 1988. Improved staining of proteins in polyacrylamide gel including isoelectric focusing gels with clear background at nanogram sensitivity using comassie brilliant blue G-250 and R-250. Electrophoresis. 9:255-262.
Nishimoto, S., Hashimoto, A. A., Seki, N., Kimure, I., Toyoda, K., Fujita,T. and Arai, K. 1987. Influencing factors on changes in myosin heavy chain and jelly strength of salted meat paste from Alaska pollack during setting. Nippon Suisan Gakkaishi. 53:2011-2020.
Niwa, E. 1975. Role of hydrophobic bonding in gelation of fish flesh paste. Bull. Jap. Soc. Sci. Fish. 41:773.
Niwa, E. 1992. Chemistry of surimi gelation. In “Surimi Technology”. pp.389-427. Lanier, T. C., ed. Marcel Dekker. 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., Kohda, S. I., Kanoh, S. and Nakayama, T. 1986a. Exposure of hydrophobic amino acid residues from actomyosin on freezing reconfirmation by fluorometry. Bull. Jap. Soc. Sci. Fish. 52:1039-1046.
Niwa, E., Kohda, S. I. and Nakayama, T. 1986b. Freezing induced exposure of hydrophobic amino acid residues from actomyosin. Bull. Jap. Soc. Sci. Fish. 52:859-862.
Niwa, E., Kohda, S., Osaka, Y., Nakayama, T., Wetabe, S. and Hashimoto, K. 1989. Changes in surface hydrophobic of fish actomyosin induced by urea. Nippon Suisan Gakkaishi. 55:143-146.
Niwa, E., Matsubara, Y. and Hamada, I. 1982a. Hydrogen and other polar bonding in fish flesh gel and setting. Bull. Jap. Soc. Sci. Fish. 48:667.
Niwa, E., Matsubara, Y., Nakayama, T. and Hamada, I. 1982b. Participation of SS bonding in the appearance of setting. Bull. Jap. Soc. Sci. Fish. 48:727.
Niwa, E., Suzuki, M. and Nakayama, T. 1985. Heat-induced polymerization of fish actomyosin. Bull. Jap. Soc. Sci. Fish. 51:795.
Noguchi, S. 1974. The control of denaturation of fish muscle proteins during frozen storage. Doctoral Dissertation Sophia Univ.,Tokyo, Japan.
Noguchi, S. and Matsumoto, J. J. 1970. Studies on the control of the denaturation of the fish muscle proteins during frozen storage. Bull. Jap. Soc. Fish. 37:1115.
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 effct of two-step heating on the meat pastes from different fish in modori-indcing conditions. Nippon Suisan Gakkaishi. 60:667.
Nowsad, A. A. K. M., Kanoh, S. and Niwa, E. 2000. Thermal gelation characteristics of breast and thigh muscles of spent hen and broiler and their surimi. Meat Sci. 54(2):169-175.
Numakura, T., Seki, N., Kimura, I., Totoda, K., Fujita, K., Takama, K. and Arai, K. 1985. Cross-linking reaction of myosin in the fish paste during setting. Bull. Jap. Soc. Sci. Fish. 51:1559-1565.
Oguni, M., Inoue, N., Ohi, K. and Shinano, H. 1987. Denaturation of crap myosin B during frozen and supercooled storage at -8℃. Nippon Suisan Gakkaishi.
Oguni, M., Kubo, T. and Matsumito, J. J. 1975. Studies on the denaturation of fish muscle proteins I. Physicochemical and electron microscopical studies of freeze denatured of carp actomyosin. Bull. Jap. Soc. Sci. Fish. 41:1113-1123.
Ohta, F. 1985. An evaluation of effect of temperature on danaturation of protein in frozen KCl solution. Nippon Suisan Gakkaishi. 51:505.
Okada, T., Ohta, F., Inoue, N. and Akiba, M. 1985. Denaturation of carp myosin B in KCl solution during frozen storage. Nippon Suisan Gakkaishi. 51:1887.
Okata, M., Yokoseki, M. and Nunoaki, T. 1974. Minced fish meat products (Gyoniku Neriseihin, in Japanese) pp.374, Koseisha, Tokyo.
Park, J. W. 1994. Functional protein additives in surimi gels. J. Food Sci. 59:525-527.
Park, S., Brewer, M. S., Mckeith, F. K., Bechtel, P. J. and Novakofski, J. 1996. Salt, cryoprotectants and preheating temperature effects on surimi-like material from beef or pork. J. Food Sci. 61:790-795.
Ragnarsson, K. and Regensstein, L. M. 1989. Changes in electrophoretic patterns of gadoid and non-gadoid fish muscle during frozen storage. J. Food Sci. 54: 819-823.
Seki, N. 1992. Effects of salts on transglutaminase-mediated cross-linking of myosin in suwari gel from walleye pollack. Nippon Suisan Gakkaishi. 58:2181-2187.
Shimada, K. and S. Matsushita. 1980. Thermal coagulation of egg albumin. J. Agric, Food Chem. 28:409-414.
Shimizu, Y. and Nishioka, F. 1974. Interactions between horse mackerel actomyosin and sarcoplasmic proteins during heat coagulation. Bull. Jap. Soc. Sci. Fish. 40:231.
Shimizu, Y., Machida, R. and Takenami, S. I. 1981. Species variations in the gel-forming characteristics of fish meat paste. Bull. Jap. Soc. Sci. Fish. 47: 95-101.
Shimizu, Y., Nomura, A. and Nishioka, F. 1986. Modori (fish gel degradation occurring at a around 60℃) inducing property of croaker myosin preparation. Nippon Suisan Gakkaishi. 52:2023-2027.
Siegel, D. G. and Schmidt, G. R. 1979. Ionic, pH, and temperature effects on the binding ability of myosin. J. Food Sci. 44:1686-1690.
Sikorski, Z. 1978. Protein changes in muscle foods due to freezing and frozen storage. Int. J. Refrigeration. 1:173-176.
Sikorski, Z. E. and Pan, B. S. 1994. Preservation of seafood quality. In “Seafood: Chemistry, Processing Technology and Quality”. pp.168-195. ed. by F. Shahidi and J. R. Botta.
Sikorski, Z., Olley, J. and Kostuch, S. 1976. Protein changes in frozen fish. Crit. Rev. Food Sci. Nutri., CRC Press, New York. 8:97-129.
Singh, R. and Wang, C. Y. 1977. Quality of frozen food. a review. J. Food Proc. Eng. 1:97.
Sun, C. T. 1981. Water behavior and functionality of frozen dolphin-fish mince. Doctorate, Dept. Agric. Chem., Natl. Taiwan Unvi., Taipei, Taiwan, R.O.C.
Suzuki, T. 1967. Freezing denaturation of fish protein. Refrigeration (Japan). 42(471):46.
Suzuki, T. 1981. Fish and krill proteins, Processing Technology. pp.1-5, Applied Science Publishers. Ltd., London.
Suzuki, T., Kanna, K. and Tanaka, T. 1964. Studies on protein denaturation of frozen fish comparison between rapid freezing by liquid nitrogen (-196℃) and air (-20℃) freezing. Nippon Suisan Gakkaishi. 30:1022.
Taguchi, T., Tanaka, M. and Suzuki, K. 1983. Effect of alcohols on “himodori” (thermally induced gel disintegration) in oval filefish meat paste. Nippon Suisan Gakkaishi. 49:1149-1151.
Tanikawa, E., Akiba, E., and Shitamori, A. 1963. Cold storage of cod fillets treated with polyphosphate. Food Technol. 17:1425.
Taso, C. Y. 1981. Studies on the denaturation of muscle proteins of mackerel and amberfish during frozen storage. Masters thesis, Dept. Marine Food Sci., Natl. Taiwan Collage of Marine Sci. & Technol., Taiwan, R.O.C.
Taso, C. Y., Chou, K.C. and Jiang, S. T. 1980. Studies on freezing reservation of raw material of minced fish meat products I. J. Chinese Agri, Chem. Soc. 18(1-2):77.
Toyohara H. and Shimizu, Y. 1988. Relation between the modori phenomenon and myosin heavy chain breakdown in threadfin-bream gel. Agric. Biol. Chem. 255-257.
Toyohara, H., Sasaki, K., Kinoshita, M. and Shimizu, Y. 1990. Effect of bleeding on the modori-phenomenon and possible existence of some modori-inhibitor(s) in serum. Nippon Suisan Gakkaishi. 56:1245-1249.
Toyohara, H., Sasaki, K., Kinoshita, M., Shimizu, Y. and Sakaguchi, M. 1991. Detection of inhibitors for modori-inducing proteinase in fish and calf serums. Nippon Suisan Gakkaishi. 57:521-525.
Tsuchiya, T., Tsuchiya, Y., Nonomura, Y. and Matsumoto, J. J. 1975. Prevention of freeze denaturation of carp actomyosin by sodium glutamate. J. Biochem. 77:853-862.
Tsukamasa, Y., Sato, K., Shimizu, Y., Imai, C., Sugiyama, M., Minegishi, Y. and Kawabata, M. 1993. ε-(γ-glutamyl)lysine cross-link formation in sardine myofibril sol during setting at 25℃. J. Food Sci. 58:785-787.
Tsuyuki, H. and Roberts, E. 1966. Inter-species relationships within the genus Oncorhynchus based on biochemical systematics. J. Fish. Res. Bd. Canada 23:101.
Wasson, D. H., Reppond, K. D., Babbitt, J. K. and French, J. S. 1992. Effect of additives on proteolytic and functional properties of arrowtooth flounder surimi. J. Aquatic Food Product Technol. 1:147-165.
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.
Woods, E. F. 1967. Molecular weight and subunit structure of tropomysion B. J. Biol. Chem. 242(12):2859.
Wu, C. H. 1983. Recovery of protein from the leaching waste water of frozen surimi by acid coagulation. Bull. Taiwan Fish. Res. Inst. 35:252.
Yamamoto, Y., Nanbu, S. and Arai, K. 1992. Gel forming ability of walleye pollack surimi containing sugar and carboxylic acid salt. Nippon Suisan Gakkaishi. 58:759-766.
Yokoyama, M. 1969. Studies on adhesion of fish meat products on casing in fish sausage and kamaboko-II. Effect of different species of fish and their grade of freshness on the rate of adhesion. Bull. Jap. Soc. Sci. Fish. 35:199-205.
Yoshinaka, R., Shiraishi, M. and Ikeda, S. 1972. Effect of ascorbic acid on the gel formation of fish meat. Bull. Jap. Soc. Sci. Fish. 38:511.

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