title: Participation of cysteine protease cathepsin L in the gel disintegration of red bulleye (Priacanthus macracanthus) surimi gel paste.
abstract: BACKGROUND
  Endogenous proteases, among them cysteine-type proteases, are reported to contribute to gel disintegration, resulting in kamaboko of poor quality. Severe gel disintegration occurs in red bulleye surimi gel paste. The objective of this study was to clarify the participation of cysteine protease cathepsin L in the gel disintegration of red bulleye surimi. The surimi was made into kamaboko with and without cathepsin L inhibitors. To confirm its hydrolysis action, crude cathepsin L was also extracted and added to the surimi to make kamaboko.
  
  
  RESULTS
  The gel strength of kamaboko obtained by both one-step (50 degrees C, 2 h) and two-step (50 degrees C, 2 h + 80 degrees C, 20 min) heating was very low in the absence of inhibitors. Protease inhibitors E-64 and leupeptin were found to enhance the gel strength considerably. Sodium dodecyl sulfate polyacrylamide gel electrophoresis revealed that the hydrolysis of kamaboko was promoted by crude cathepsin L and inhibited by E-64 and leupeptin. The gel strength of two-step heated kamaboko was increased from 12 to 110 and 130 g cm(-2) by E-64 and leupeptin respectively at a concentration of 0.2 g kg(-1) surimi.
  
  
  CONCLUSIONS
  Endogenous cathepsin L of red bulleye surimi participates in gel disintegration during kamaboko processing. It does so by degrading the myosin heavy chain of actomyosin and consequently hindering the gelation of red bulleye surimi.
authors.affiliation: Department of Food Science and Nutrition, Zhejiang University, Hangzhou, China. yqhu@zju.edu.cn
authors.forename: Yaqin
authors.initials: Y
authors.lastname: Hu
authors.forename: Katsuji
authors.initials: K
authors.lastname: Morioka
authors.forename: Yoshiaki
authors.initials: Y
authors.lastname: Itoh
mesh_terms: D000818:Animals; D056668:Cathepsin L / Q000378:metabolism*; D057056:Cysteine Proteases / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D005396:Fish Products / Q000592:standards*; D029941:Fish Proteins / Q000378:metabolism*; D005782:Gels / Q000737:chemistry; D006358:Hot Temperature; D006868:Hydrolysis; D007930:Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D007976:Leupeptins / Q000494:pharmacology; D010473:Perciformes; D011480:Protease Inhibitors / Q000494:pharmacology
chemical_list: D029941:Fish Proteins; D005782:Gels; D007976:Leupeptins; D011480:Protease Inhibitors; D057056:Cysteine Proteases; D056668:Cathepsin L; D007930:Leucine; C032854:leupeptin; C024974:E 64