ISSN:
1750-3841
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
Intact fibrils (a), actin- and tropomyosin-poor fibrils (b), and synthetic fibrils (c) were prepared from beef M. semitendinosus within 2 hr. of slaughter. Myosin A was prepared from rabbit muscle. The three kinds of fibrils were incubated at 35°C with a trace of toluene. Then the binding quality of sausage prepared from these materials at regular intervals was examined by estimation of elasticity in connection with other physicochemical properties. In (a) and (b), the changes in the binding were in fair agreement with those characteristic of whole muscle sausage made immediately after death. On the other hand, the changes in binding in (c) resembled in many ways those of whole muscle used after storage at 4°C for 7 days after death. Hence, actin and tropomyosin do not greatly influence the binding quality of sausage. It could not be shown that the amount nitrogen soluble in Weber-Edsall solution of 0.6M NaCl, or that pH value or water-holding capacity directly influenced the binding quality of the finished products. The course of inactivation of ATPase observed when fibrils were incubated was very similar to that of typical myosin R (in which denaturation takes place in two fairly distinct stages), resembling especially the first stage of the denaturation reaction. From the observation that the first stage of the denaturation of myosin B-ATPase was due to the denaturation of myosin A contained in the preparation, it was concluded that the myosin A present in fibrils is an important substance exerting great influence on the binding quality of sausage.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1365-2621.1961.tb00368.x
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