作者: Amin Oujifard , Soottawat Benjakul , Mehraj Ahmad , Jafar Seyfabadi
DOI: 10.1016/J.LWT.2012.01.016
关键词:
摘要: Abstract Impact of bambara groundnut protein isolate (BGPI) on autolysis and gel properties surimi from threadfin bream ( Nemipterus bleekeri ) was investigated. BGPI with trypsin inhibitory activity 6356.3 ± 6.02 unit/g markedly increased P 0.05 the breaking force deformation modori as levels used (0–3 g/100 g) increased. Nevertheless, only 0.25 g/100 g kamaboko gel increasing showed detrimental effect gelation. Myosin heavy chain (MHC) more retained when concentration increased, especially in gel. However, whiteness slightly decreased levels. Microstructure kamaboko added had finer ordered fibrillar structure than that without addition. Therefore, at an appropriate level could be alternative food-grade inhibitor to improve surimi.