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Participation of cysteine protease cathepsin L in the gel disintegration of red bulleye (Priacanthus macracanthus) surimi gel paste.
J Sci Food Agric. 2010 Feb; 90(3):370-5.JS

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.

CONCLUSION

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.

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Authors+Show Affiliations

Hu Y
Department of Food Science and Nutrition, Zhejiang University, Hangzhou, China. yqhu@zju.edu.cn
Morioka K
No affiliation info available
Itoh Y
No affiliation info available

MeSH

AnimalsCathepsin LCysteine ProteasesElectrophoresis, Polyacrylamide GelFish ProductsFish ProteinsGelsHot TemperatureHydrolysisLeucineLeupeptinsPerciformesProtease Inhibitors

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

20355055

Citation

Hu, Yaqin, et al. "Participation of Cysteine Protease Cathepsin L in the Gel Disintegration of Red Bulleye (Priacanthus Macracanthus) Surimi Gel Paste." Journal of the Science of Food and Agriculture, vol. 90, no. 3, 2010, pp. 370-5.
Hu Y, Morioka K, Itoh Y. Participation of cysteine protease cathepsin L in the gel disintegration of red bulleye (Priacanthus macracanthus) surimi gel paste. J Sci Food Agric. 2010;90(3):370-5.
Hu, Y., Morioka, K., & Itoh, Y. (2010). Participation of cysteine protease cathepsin L in the gel disintegration of red bulleye (Priacanthus macracanthus) surimi gel paste. Journal of the Science of Food and Agriculture, 90(3), 370-5. https://doi.org/10.1002/jsfa.3819
Hu Y, Morioka K, Itoh Y. Participation of Cysteine Protease Cathepsin L in the Gel Disintegration of Red Bulleye (Priacanthus Macracanthus) Surimi Gel Paste. J Sci Food Agric. 2010;90(3):370-5. PubMed PMID: 20355055.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Participation of cysteine protease cathepsin L in the gel disintegration of red bulleye (Priacanthus macracanthus) surimi gel paste. AU - Hu,Yaqin, AU - Morioka,Katsuji, AU - Itoh,Yoshiaki, PY - 2010/4/1/entrez PY - 2010/4/1/pubmed PY - 2010/9/10/medline SP - 370 EP - 5 JF - Journal of the science of food and agriculture JO - J Sci Food Agric VL - 90 IS - 3 N2 - 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. CONCLUSION: 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. SN - 1097-0010 UR - https://www.unboundmedicine.com/medline/citation/20355055/Participation_of_cysteine_protease_cathepsin_L_in_the_gel_disintegration_of_red_bulleye__Priacanthus_macracanthus__surimi_gel_paste_ L2 - https://doi.org/10.1002/jsfa.3819 DB - PRIME DP - Unbound Medicine ER -