In recent years Takifugu rubripes has been increasingly popular among people base on its good taste. Cathepsin L was related to the formation of amino acids and small peptides. This study described the biochemical characterization of Cathepsin L and its role in the taste formation of Takifugu rubripes. Cathepsin L gene from Takifugu rubripes tissues was cloned successfully, and Cathepsin L with molecular masses of 46 kDa was isolated and enzymatically characterized. This enzyme reached its highest activity at 40 °C and pH 5.5. Cu2+ and Mn2+ ions reduced the activity of Cathepsin L, but Fe3+ and Ca2+ ions prominently increased its activity when the final concentrations of metal ions were 1 mM and 5 mM, respectively. The addition of phenylmethanesulfonyl fluoride gradually decreased the enzyme activity over 0.5 mM. 200–3000 KDa fraction from Takifugu rubripes muscle after Cathepsin L hydrolysis showed the stronger kokumi and umami taste, especially kokumi. In this study, the recombinant Cathepsin L from Takifugu rubripes could play a role in flavor formation and be applied in flavor studies through the degradation of animal proteins.
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A.J. Barrett, Controversies in Neuro-urology (Wiley, New Jersey, 2008), pp. 3–16
J. Liu, G.K. Sukhova, J.T. Yang, J.S. Sun, L.K. Ma, A. Ren, W.H. Xu, H.X. Fu, G.M. Dolganov, C.C. Hu, P. Libby, G.P. Shi, Atherosclerosis 184(2), 302–311 (2006)
I. Whang, M. De Zoysa, C. Nikapitiya, Y. Lee, Y. Kim, S. Lee, C. Oh, S.J. Jung, M.J. Oh, C.Y. Choi, S.Y. Yeo, B.S. Kim, S.J. Kim, J. Lee, Fish Shellfish Immunol. 30(3), 763–772 (2011)
Q.H. Li, J.Q. Ao, Y.N. Mu, Z.J. Yang, T. Li, X. Zhang, X.H. Chen, Fish Shellfish Immunol. 47(2), 743 (2015)
J.Z. Liang, Y.Z. Rao, Z.R. Lun, T.B. Yang, Fish Physiol. Biochem. 38(6), 1795–1806 (2012)
Y.X. Sun, L. Tang, P. Wang, M.N. Abbas, J.W. Tian, B.J. Zhu, C.L. Liu, Dev. Comp. Immunol. 78, 114–123 (2018)
L.S. Dai, S.H. Chu, X.M. Yu, Y.Y. Li, Fish Shellfish Immunol. 71, 246–254 (2017)
W.J. Wang, L. Long, L. Wang, C.H. Tan, X.F. Fei, L.S. Chen, Q. Huang, Z.Q. Liang, Cancer Lett. 371(2), 274–284 (2016)
K.L. Mattock, P.J. Gough, J. Humphries, K. Burnand, L. Patel, K.E. Suckling, F. Cuello, C. Watts, M. Gautel, M. Avkiran, A. Smith, Atherosclerosis 208(1), 83–89 (2010)
Y. Zhong, J. Zhao, Y.J. Gu, Y.F. Zhao, Y.W. Zhou, G.X. Fu, Arch. Gerontol. Geriat. 61(2), 285–288 (2015)
L.A. Pennacchio, Science 2(5256), 1731–1734 (1996)
P. Taupin, J. Ray, W.H. Fischer, S.T. Suhr, K. Hakansson, A. Grubb, F.H. Gage, Neuron 28(2), 385–397 (2000)
J. Palomino, G. Herrera, J. Torres-Fuentes, P. Dettleff, A. Patel, V. Martinez, Anim. Reprod. Sci. 180, 23–29 (2017)
F. Toldra, M.N. Flores, Crit. Rev. Food Sci. 38(4), 331 (1998)
R. Cheret, C. Delbarre-Ladrat, M. de Lamballerie-Anton, V. Verrez-Bagnis, Food Chem. 101(4), 1474–1479 (2007)
L.S. Song, B.Z. Liu, J.H. Xiang, P.Y. Qian, Mar. Biotechnol. 3(4), 398–406 (2001)
M.X. Zhang, X.C. Wang, Y. Liu, X.L. Xu, G.H. Zhou, Food Chem. 135(3), 1463–1470 (2012)
M.X. Zhang, X.C. Wang, Y. Liu, X.L. Xu, G.H. Zhou, Sensors 12(9), 12562–12571 (2012)
M. Wang, X.Y. Zhang, R.R. Guo, Z.P. Cai, X.C. Hu, H. Chen, S. Wei, J. Voglmeir, L. Liu, Carbohyd. Res. 457, 1–7 (2018)
M. Flores, M.C. Aristoy, T. Antequera, J.M. Barat, F. Toldra, Meat Sci. 82(2), 241–246 (2009)
X.Q. Yu, L.J. Zhang, X.D. Miao, Y.Y. Li, Y. Liu, Food Chem. 221, 599–605 (2017)
X. Niu, M.J. Guiltinan, Nucleic Acids Res. 22(23), 4969–4978 (1994)
A.K. Mohanty, M.C. Wiener, Protein Expr. Purif. 33(2), 311–325 (2004)
R.M. Nepal, S. Mampe, B. Shaffer, A.H. Erichson, P. Bryant, Int. Immunol. 18(6), 931–939 (2006)
F. Lecaille, E. Authie, T. Moreau, C. Serveau, F. Gauthier, G. Lalmanach, Eur. J. Biochem. 268(9), 2733 (2001)
K. Schilling, S. Pietschmann, M. Fehn, I. Wenz, B. Wiederanders, Biol. Chem. 382(5), 859 (2001)
M.C. Hughes, E.E. Neill, P.L.H. McSweeney, Food Chem. 64(4), 525–530 (1999)
F. Shahidi, Y.V.A.J. Kamil, Trends Food Sci. Tech. 12(12), 435–464 (2001)
D.P. Bown, H.S. Wilkinson, M.A. Jongsma, J.A. Gatehouse, Insect Biochem. Mol. 34(4), 305–320 (2004)
Y.Y. Tian, E. Umezawa, R. Duan, K. Konno, Fisheries Sci. 76(2), 365–373 (2010)
T. Yoonuan, S. Nuamtanong, P. Dekumyoy, O. Phuphisut, P. Adisakwattana, Parasitol. Res. 115(12), 4457–4470 (2016)
N. Rotzoll, A. Dunkel, T. Hofmann, J. Agr. Food Chem. 53(10), 4149–4156 (2005)
O. Frank, H. Ottinger, T. Hofmann, J. Agr. Food Chem. 49(1), 231–238 (2001)
M.R. Kim, Y. Kawamura, K.M. Kim, H. Cherl, M.R. Lee, J. Agr. Food Chem. 56(14), 5852–5858 (2008)
This work was funded by The National Key R&D Program of China (2016YFD0400803, 2016YFD0401501) and National Natural Science Foundation of China (Grant Nos. 31622042, 31371790, 31271900).
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Tang, Q., Wang, W., Zhang, L. et al. Cloning, purification and biochemical characterization of recombinant Cathepsin L from Takifugu rubripes and its role in taste formation. Food Measure 14, 485–491 (2020). https://doi.org/10.1007/s11694-019-00122-7
- Takifugu rubripes
- Cathepsin L
- Biochemical characterization
- Flavor peptides