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Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys olivaceus) Surimi Gel.
Molecules. 2021 Mar 28; 26(7)M

Abstract

We investigated the effect of endogenous cathepsin L on surimi gel produced from olive flounder (Paralichthys olivaceus). The amino acid sequences of six proteins predicted or identified as cathepsin L were obtained from the olive flounder genome database, and a phylogenetic analysis was conducted. Next, cathepsin L activity toward N-α-benzyloxycarbonyl-l-phenylalanyl-l-arginine-(7-amino-4-methylcoumarin) (Z-F-R-AMC) was detected in crude olive flounder extract and a crude enzyme preparation. A considerable decrease in the level of myosin heavy chain (MHC) in surimi occurred during autolysis at 60 °C. In contrast, the levels of actin, troponin-T, and tropomyosin decreased only slightly. To prevent protein degradation by cathepsin L, a protease inhibitor was added to surimi. In the presence of 1.0% protease inhibitor, the autolysis of olive flounder surimi at 60 °C was inhibited by 12.2%; the degree of inhibition increased to 44.2% as the inhibitor concentration increased to 3.0%. In addition, the deformation and hardness of modori gel increased as the inhibitor concentration increased to 2.0%. Therefore, cathepsin L plays an important role in protein degradation in surimi, and the quality of surimi gel could be enhanced by inhibiting its activity.

Authors+Show Affiliations

Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Korea.Research Institute of Agriculture and Life Sciences, Seoul National University, Seoul 08826, Korea. Department of Agricultural Biotechnology, Seoul National University, Seoul 08826, Korea. Center for Food and Bioconvergence, Seoul National University, Seoul 08826, Korea. Center for Agricultural Microorganism and Enzyme, Seoul National University, Seoul 08826, Korea.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

33800606

Citation

Kwon, Chang Woo, and Pahn-Shick Chang. "Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys Olivaceus) Surimi Gel." Molecules (Basel, Switzerland), vol. 26, no. 7, 2021.
Kwon CW, Chang PS. Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys olivaceus) Surimi Gel. Molecules. 2021;26(7).
Kwon, C. W., & Chang, P. S. (2021). Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys olivaceus) Surimi Gel. Molecules (Basel, Switzerland), 26(7). https://doi.org/10.3390/molecules26071901
Kwon CW, Chang PS. Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys Olivaceus) Surimi Gel. Molecules. 2021 Mar 28;26(7) PubMed PMID: 33800606.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Role of Endogenous Cathepsin L in Muscle Protein Degradation in Olive Flounder (Paralichthys olivaceus) Surimi Gel. AU - Kwon,Chang Woo, AU - Chang,Pahn-Shick, Y1 - 2021/03/28/ PY - 2021/02/09/received PY - 2021/03/11/revised PY - 2021/03/22/accepted PY - 2021/4/3/entrez PY - 2021/4/4/pubmed PY - 2021/5/18/medline KW - cathepsin L KW - cathepsin L inhibition KW - olive flounder (Paralichthys olivaceus) KW - protein degradation KW - surimi JF - Molecules (Basel, Switzerland) JO - Molecules VL - 26 IS - 7 N2 - We investigated the effect of endogenous cathepsin L on surimi gel produced from olive flounder (Paralichthys olivaceus). The amino acid sequences of six proteins predicted or identified as cathepsin L were obtained from the olive flounder genome database, and a phylogenetic analysis was conducted. Next, cathepsin L activity toward N-α-benzyloxycarbonyl-l-phenylalanyl-l-arginine-(7-amino-4-methylcoumarin) (Z-F-R-AMC) was detected in crude olive flounder extract and a crude enzyme preparation. A considerable decrease in the level of myosin heavy chain (MHC) in surimi occurred during autolysis at 60 °C. In contrast, the levels of actin, troponin-T, and tropomyosin decreased only slightly. To prevent protein degradation by cathepsin L, a protease inhibitor was added to surimi. In the presence of 1.0% protease inhibitor, the autolysis of olive flounder surimi at 60 °C was inhibited by 12.2%; the degree of inhibition increased to 44.2% as the inhibitor concentration increased to 3.0%. In addition, the deformation and hardness of modori gel increased as the inhibitor concentration increased to 2.0%. Therefore, cathepsin L plays an important role in protein degradation in surimi, and the quality of surimi gel could be enhanced by inhibiting its activity. SN - 1420-3049 UR - https://www.unboundmedicine.com/medline/citation/33800606/Role_of_Endogenous_Cathepsin_L_in_Muscle_Protein_Degradation_in_Olive_Flounder__Paralichthys_olivaceus__Surimi_Gel_ L2 - https://www.mdpi.com/resolver?pii=molecules26071901 DB - PRIME DP - Unbound Medicine ER -