Studies on application of transglutaminase to meat and meat products Part II. The effect of microbial transglutaminase on gelation of myosin B, myosin and actin.

DOI

Bibliographic Information

Other Title
  • 肉および肉製品へのトランスグルタミナーゼの応用に関する研究（第２報）　ミオシンＢ，ミオシンおよびアクチンのゲル化に及ぼす微生物由来トランスグルタミナーゼの影響
  • Studies on Application of Transglutaminase to Meat and Meat Products Part II

Description

Myosin B, myosin and actin were polymerized and gelled by Ca2+-independent transglutaminase (B.T.G.) derived from a microorganism (Streptoverticillium). The concentration of B.T.G. required for gelation of myosin B was lower than that for myosin and actin. On SDS-PAGE of myosin B treated with B.T.G., the monomeric myosin heavy chain decreased markedly with increasing amount of B.T.G. and a polymer fraction increased. Analysis of actin by SDS-PAGE indicated that actin was also polymerized. The small amount of B.T.G. increased the turbidity of myosin B induced by heating of linearly increasing rate of 2°C/min, suggesting that myosin B suspension with B.T.G. formed a finer network structure of heat-induced gel than that of myosin B alone. When the myosin B solution with B.T.G. was heated and then the heat induced gel centrifuged; tropomyosin and troponin-T were not freed from the sediment. These results suggest that the regulatory proteins play some role in the heat-induced gelation of this system.

Journal

Details 詳細情報について

  • CRID
    1390001206406290688
  • NII Article ID
    130003788863
  • DOI
    10.3136/nskkk1962.37.6_446
  • ISSN
    00290394
  • Text Lang
    ja
  • Data Source
    • JaLC
    • Crossref
    • CiNii Articles
  • Abstract License Flag
    Disallowed

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