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Effect of microbial transglutaminase on autolysis and gelation of lizardfish surimi
Author(s) -
Yongsawatdigul Jirawat,
Piyadhammaviboon Penprapha
Publication year - 2005
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.2149
Subject(s) - autolysis (biology) , chemistry , food science , tropomyosin , fish <actinopterygii> , tissue transglutaminase , fish meal , myosin , biochemistry , enzyme , biology , fishery
In the absence of microbial transglutaminase (MTGase), the textural properties of lizardfish surimi ( Saurida spp) improved when pre‐incubated at 4 and 25 °C for 24 and 4 h, respectively. MTGase optimally catalyzed incorporation of monodansylcadaverine (MDC) into surimi at 40 °C. Addition of MTGase appeared to reduce autolytic activity at 25 and 40 °C, but had no effect on autolytic activity at 65 °C. Breaking force and deformation of lizardfish surimi significantly improved when 0.1 unit MTGase g −1 surimi (1.8 g kg −1 ) was added and pre‐incubated at either 25 or 40 °C. Textural properties improved concomitant with cross‐linked polymers of myosin heavy chain and tropomyosin, but not actin. Addition of MTGase also improved the storage modulus ( G ′). The gel network of surimi mixed with MTGase and pre‐incubated at 40 °C readily formed during the pre‐incubation period, while formation of the gel network began at 48.1 °C in the absence of MTGase. Copyright © 2005 Society of Chemical Industry

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