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Abstract
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Impact of bambara groundnut protein isolate (BGPI) on autolysis and gel properties of surimi from
threadfin bream (Nemipterus bleekeri) was investigated. BGPI with trypsin inhibitory activity of
6356.3 6.02 unit/g markedly increased (P < 0.05) the breaking force and deformation of modori gel as
the levels used (0e3 g/100 g) increased. Nevertheless, only 0.25 g/100 g BGPI increased breaking force
and deformation of kamaboko gel and increasing BGPI levels showed detrimental effect on gelation.
Myosin heavy chain (MHC) was more retained when BGPI concentration increased, especially in modori
gel. However, whiteness slightly decreased (P < 0.05) with increasing BGPI levels. Microstructure of
kamaboko gel added with 0.25 g/100 g BGPI had finer and more ordered fibrillar structure than that
without BGPI addition. Therefore, BGPI at an appropriate level could be an alternative food-grade
inhibitor to improve gel properties of surimi.
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