著者

志水 寛

出版者

一般社団法人 日本調理科学会

雑誌

調理科学 (ISSN:09105360)

巻号頁・発行日

vol.24, no.4, pp.322-328, 1991-11-20 (Released:2013-04-26)

参考文献数

15

著者

西岡 不二男 町田 律 志水 寛

出版者

日本水産學會

雑誌

日本水産学会誌 (ISSN:00215392)

巻号頁・発行日

vol.49, no.8, pp.1233-1238, 1983

被引用文献数

3 11

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The dolphinfish myosin (purity 92%) was compared with respect to the kamaboko-forming ability atomyosin (myosin moiety 70%), myofibrils (myosin moiety 72%) and minced meat (myosin content 32%) prepared from the same specie. Kamaboko jelly from the dolphinfish myosin was diferet with regard to others, in that it was transparent, light blueish and much more elasticl The strength of myosin jelly was 3.0, 2.6 and 44 times more than that of actomyosin, myofibrils and minced meat jelly having the same moisture content (86%), showing that the kamaboka-forming ability of those materials are solely dependent on their myosin moiety content, CM. It was found that the tensile strength of the jellies can be expresed as a function of C_M, S=k•C_Mⁿ (k, n are constants), while hte breaking extension is decreased with the concentration of moieties other than myosin.

著者

志水 寛 柄多 哲 西岡 不二男

出版者

公益社団法人 日本水産学会

雑誌

日本水産学会誌 (ISSN:00215392)

巻号頁・発行日

vol.42, no.9, pp.1025-1031, 1976-09-25 (Released:2008-02-29)

参考文献数

12

被引用文献数

11 12

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The extractability of proteins from fish muscle homogenates was investigated at ionic strengths ranging between μ 0 and 0.3 (pH 6.8 ?? 7.0; ratio of muscle to extractant, 1:30) with 18 species of teleosts. Species variations were observed in the extraction patterns obtained between μ 0 and 0.05. As the ionic concentration was raised from μ 0 to 0.05, the amount of extractable protein increased rapidly in dark meat fish (migratory fish) such as sardine or chub mackerel and increased slowly in fish such as horse mackerel or lizard fish which are considered to be intermediate between dark and white meat fish. In white meat fish (bottom fish) such as Alaska pollack or nemipterid, however, the extractabilities more or less dcreased in the range of μ 0.025-0.05.Such differences between dark and white meat fish are attributable to a fraction eluting at Kav 0.2 ?? 0.3 on Sephadex G 200 filtration which is abundant in the sarcoplasm of the former (chub mackerel), and the greater solubilization of myofibrils from the latter (Alaska pollack) at ionic strengths of μ 0.025. From the results, μ 0.05 was recommended as the optimum concentraion for extracting sarcoplasmic proteins from either dark or white meat fish. The values of 0.05μ extractable protein nitrogen obtained in this study closely corresponded with those of non-protein nitrogen, the latter being an accepted marker for distinguishing between the two groups of fish.

著者

志水 寛 吉本 晴樹 清水 亘

出版者

公益社団法人 日本水産学会

雑誌

日本水産学会誌 (ISSN:00215392)

巻号頁・発行日

vol.28, no.6, pp.610-615, 1962-06-25 (Released:2008-02-29)

参考文献数

7

被引用文献数

3 4

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A sticky paste, prepared by braying fish meat with 2 or 3% NaCl, turns to a tough and elastic gel, “kamaboko”, on cooking processes, such as steaming, boiling, or broiling. It has been experienced that if the processes are unsuccessfully conducted rather fragile gels sometimes yield. In the previous paper, the authors showed that in such cases the paste should be kept for a long time at a temperature range between 50°C and 60°C., the kamaboko gel lost its elasticity and became fragile. In the present study, such phenomenon, the collapse of gel structure during cooking, was observed. Samples used were lizard fish meat paste packed in Kurehalon tubus of diameter 3cm. (Kureha Kasei Co., Ltd.), and the cooking was made in water bathes kept at various temperatures. Gel-strength was evaluated by the magnitude of the tensile strength of a ring-shaped specimen (Fig. 1) and also the score values obtained by an organoleptic test in 10-point scale. Results are summarized as follows: (1) Lowering in the gel-strength during cooking occurred at higher temperatures than 50°C., favourably near at around 60°C. and again at 90°C. (Fig. 2). (2) Washing process on the raw chopped meat, by which a greater part of the water soluble matters was removed, raised the kamaboko-forming capacity of the meat paste, but had little effects on the change in gel-strength at 60°C. (Fig. 3). This may suggest that the water-soluble matters in the paste play a minor role in this phenomenon. (3) Meat pastes brayed of aged meat (stored for 5 days at 4°-5°C.) were more easily subjected to the heat influence at 60°C. than those of fresh meat (Fig. 3). (4) Initial pH of the paste seemed to have no significant influence on the occurrence of the phenomenon (Fig. 4). (5) Stability of the kamaboko gel to heating at 60°C. was quite different with the conditions, under which the paste had been kept prior to the cooking. Gels produced by pre-cooking at 80°C. and 90°C. for 20minutes did not change their strength even after heating for long time at 60°C., while those pre-cooked at lower temperatures than 70°C. were significantly damaged on the gel structure (Fig. 5).

著者

木下 政人 豊原 治彦 志水 寛

出版者

日本水産學會

雑誌

日本水産学会誌 (ISSN:00215392)

巻号頁・発行日

vol.56, no.9, pp.1485-1492, 1990

被引用文献数

14 63

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<i>Modori</i>-inducing proteinase (MIP) could be classified into four types as follows on the basis of the extractability from muscle, the optimum temperature for the activity of myosin heavy chain degradation, and the sensitivity to n-butanol. (1) Sarcoplasmic-50°C-MIP (Sp-50-MIP) which is easily extractable, acts optimally at 50°C, and is not sensitive to n-butanol, (2) sarcoplasmic-60°C-MIP (Sp-60-MIP) which is also easily extractable, acts optimally at 60°C, and is sensitive to n-butanol, (3) myofibrillar-50°C-MIP (Mf-50-MIP) which is tightly associated with myofibrils, acts optimally at 50°C, and is not sensitive to n-butanol, and (4) myofibrillar-60°C-MIP (Mf-60-MIP) which is also tightly associated with myofibrils, acts optimally at 60°C, and is sensitive to n-butanol.<br> Twelve fish species examined were classified into the following five groups according to the dis-tribution pattern of the above 4 types of MIP. (1) The species having only Sp-60-MIP, such as walleye pollack, mud dab, rainbow trout, brown croaker and red sea bream, (2) the species having both Sp-50-MIP and Sp-60-MIP, such as threadfin bream, (3) the species having both Mf-50-MIP and Mf-60-MIP, such as crucian carp, Pacific mackerel and file fish, (4) the species having both Sp-60-MIP and Mf-60-MIP, such as nibe croaker and tilpia, and (5) the species having Sp-60-MIP, Mf-50-MIP, and Mf-60-MIP, such as shortfin lizard fish.

著者

佐藤 健司 吉中 禮二 佐藤 守 志水 寛

出版者

日本水産學會

雑誌

日本水産学会誌 (ISSN:00215392)

巻号頁・発行日

vol.52, no.9, pp.1595-1600, 1986

被引用文献数

29 152

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The contents of acid-soluble and insoluble collagens in the ordinary muscle of twenty-two species of fishes was determined. In addition, the contribution of muscle collagen to the swimm-ing movement of fish and to the texture of the sliced raw meat was examined.<br> The total collagen content varied with species in the ranges from 0.34 to 2.19% of wet tissue and from 1.6 to 12.4% of crude protein. The solubility of muscle collagen of fishes was generally much higner than that reported for muscle collagen of mammals. As for the swimming movement, the results indicated that the musculature of the fish with flexible body comprises a high proportion of collagen. As for the textural properties, the results indicated that the muscle collagen con-tributes to the toughness of the sliced raw meat.

著者

志水 寛

出版者

一般社団法人 日本調理科学会

雑誌

調理科学 (ISSN:09105360)

巻号頁・発行日

vol.24, no.4, pp.322-328, 1991

著者

志水 寛

出版者

一般社団法人 日本調理科学会

雑誌

調理科学 (ISSN:09105360)

巻号頁・発行日

vol.8, no.4, pp.184-190, 1975