著者
李 南赫 加藤 登 安永 廣作 中川 則和 新井 健一
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.63, no.6, pp.977-984, 1997-11-15
被引用文献数
1 1

It is known that in the gelation of salt-ground meat from walleye pollack surimi, favorable setting temperature appears to be at around 25°C, and the changing profile of gel strength of kamaboko gel as a function of setting at 40°C varies among the preparations of frozen surimi. At a setting temperature of 40°C, there was a general trend that the breaking strength of kamaboko gel formed from high grade surimi changed in a biphasic manner: on increase at an early stage of the setting and a subsequent decrease at a later stage, while the breaking strength of the gel from low grade surimi reduced in a monophasic manner.<br>We showed that there is a good correlation between the maximum value of breaking strength of kamaboko gel attained through the setting at 25°C and the changing rate of breaking strength of kamaboko gel as a function of the setting time at 40°C.<br>On the basis of these findings, we proposed a simple and quick method for evaluating the characteristic gelling ability of walleye pollack frozen surimi for practical use in a factory.
著者
関 伸夫 宇野 秀樹 李 南赫 木村 郁夫 豊田 恭平 藤田 孝夫 新井 健一
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.1, pp.125-132, 1990
被引用文献数
39 152

When carp myosin B was incubated at 25°C, SDS-PAGE showed that an addition of a soluble extract from Alaska pollack muscle and surimi greatly stimulated the cross-linking reac-tion of myosin heavy chains. This effect was completely lost on boiling but not with dialysis, suggesting the presence of an active enzyme, transglutaminase, in the extract. It was, therefore, purified from Alaska pollack muscle by DEAE-cellulose chromatography and Sephadex G-200 gel filtration.<br> The partially purified enzyme catalyzed the cross-linking reaction of myosin heavy chain and also showed an activity to incorporate a fluorescent amine, monodansylcadaverine, into acety-lated casein. SDS-PAGE analysis of carp myosin B incubated with the enzyme in the presence of monodansylcadaverine showed several fluorescent bands, including myosin heavy chain and its polymers, with a depletion of fluorescence on actin, tropomyosin and connectin bands. The transglutaminase activity was found at a molecular weight of about 85, 000 by the gel filtration and required Ca<sup>2+</sup>.<br> From these results, the presence of transglutaminase was ascertained in Alaska pollack muscle and surimi. The setting of the salted paste of muscle or surimi may thus involve at least the enzymatic process in gel network formation.