Premium
Autolysis of Pacific White Shrimp ( Litopenaeus vannamei ) Meat: Characterization and the Effects of Protein Additives
Author(s) -
Eakpetch P.,
Benjakul S.,
Visessanguan W.,
Kijroongrojana K.
Publication year - 2008
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1750-3841.2007.00630.x
Subject(s) - autolysis (biology) , litopenaeus , shrimp , chemistry , pepstatin , food science , biochemistry , myosin , biology , enzyme , protease , fishery
Autolytic activity of Pacific white shrimp ( Litopenaeus vannamei ) mince in the absence and in the presence of 2.5%NaCl was investigated. Pacific white shrimp mince exhibited the maximum autolytic activity at 35 and 40 °C in the absence and in the presence of 2.5%NaCl, respectively, as evidenced by the highest TCA‐soluble peptide content and the greatest disappearance of myosin heavy chain (MHC). The autolysis was more pronounced in the acidic pH values, followed by alkaline pH ranges. Pepstatin A showed the highest inhibition toward autolysis in the acidic condition, revealing that aspartic proteinase was dominant in shrimp muscle. Nevertheless, soybean trypsin inhibitor effectively inhibited the autolysis at neutral and alkaline pH values, suggesting that serine proteinase was present in shrimp mince but contributed to autolysis at a lower extent in shrimp meat. Autolysis in shrimp meat could be inhibited partially by all protein additives, including bovine plasma protein (BPP), egg white (EW), and whey protein concentrate (WPC). The inhibition of autolysis increased when the level of protein additives increased with the concomitant increase in band intensity of MHC retained. WPC and BPP in the range of 2% to 3% exhibited the highest inhibition toward autolysis of shrimp mince.