Interactive effects of microbial transglutaminase and recombinant cystatin on the mackerel and hairtail muscle protein.
Interactive effects of microbial transglutaminase (MTGase) and recombinant cystatin on the mackerel and hairtail water soluble protein (WSP), salt soluble protein (SSP), and muscle protein (MP) were investigated. According to sodium dodecyl sulfate-polyacrylamide gel electrophoresis and enzymic activity analyses, cross-linking of mackerel and hairtail myosin heavy chain and low molecular mass compounds and formation of epsilon-(gamma-glutamyl)lysine cross-links were observed on samples with MTGase, while the recombinant cystatin could effectively inhibit the cathepsins and subsequently prevent degradation of proteins during setting. The cathepsins and MTGase activities in WSP, SSP, and MP solutions decreased, but the recombinant cystatin activity increased during setting at 45 degrees C.
Jiang
Shann-Tzong
ST
Department of Food Science, National Taiwan Ocean University, Keelung, Taiwan 20224, Republic of China. sjiang@mail.ntou.edu.tw
Hsieh
Jung-Feng
JF
Tsai
Guo-Jane
GJ
D000818:Animals; D002403:Cathepsins / Q000037:antagonists & inhibitors; D015891:Cystatins / Q000494:pharmacology*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D005396:Fish Products; D009124:Muscle Proteins / Q000378:metabolism*; D010473:Perciformes; D011994:Recombinant Proteins; D012995:Solubility; D011503:Transglutaminases / Q000378:metabolism*
D015891:Cystatins; D015853:Cysteine Proteinase Inhibitors; D009124:Muscle Proteins; D011994:Recombinant Proteins; D011503:Transglutaminases; D002403:Cathepsins