Abstract
Transglutaminase (TGase) plays an important role in the formation of set gel andsubsequent final surimi-based products with greater elasticity and water-holdingcapacity from salted surimi paste. In salmon surimi paste, however, the enzyme activity was inhibited even in the presence of a sufficient concentration of Ca2+ required for full activation. It was found that water soluble muscle proteins did not inhibit TGase activity, while deproteinized muscle extract markedly inhibited the enzyme activity and depressed TGase-induced cross-linking and gelationof salmon actomyosin.
The deproteinized salmon muscle extract contained a large amount of anserine as a major nitrogen compound. Anserine inhibited TGase activity, but its inhibitoryaction was slightly lower than that of the muscle extract. However, the reduction of TGase-induced cross-linking of myosin heavy chain and gelation of actomyosin by anserine was in the same extent as that by the muscle extract.
