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Mar. Drugs 2015, 13(11), 6550-6565; doi:10.3390/md13116550

Purification and Characterization of Cathepsin B from the Muscle of Horse Mackerel Trachurus japonicus

1
Graduate School of Fisheries and Environmental Sciences, Nagasaki University, Nagasaki 852-8521, Japan
2
Food Science and Technology Section, Nagasaki Prefectural Institute of Fisheries, Nagasaki 851-2213, Japan
3
College of Food and Biological Engineering, Jimei University, Xiamen 361021, China
4
Faculty of Food Nutrition, Kyushu Nutrition Welfare University, Kitakyusyu, Fukuoka 803-8511, Japan
*
Author to whom correspondence should be addressed.
Academic Editor: Takao Ojima
Received: 31 August 2015 / Revised: 11 October 2015 / Accepted: 14 October 2015 / Published: 28 October 2015
(This article belongs to the Special Issue Green Chemistry Approach to Marine Products)
View Full-Text   |   Download PDF [2843 KB, uploaded 28 October 2015]   |  

Abstract

An endogenous protease in fish muscle, cathepsin B, was partially purified and characterized from horse mackerel meat. On SDS-PAGE of the purified enzyme under reducing conditions, main protein bands were detected at 28 and 6 kDa and their respective N-terminal sequences showed high homology to heavy and light chains of cathepsin B from other species. This suggested that horse mackerel cathepsin B formed two-chain forms, similar to mammalian cathepsin Bs. Optimum pH and temperature of the enzyme were 5.0 and 50 °C, respectively. A partial cDNA encoding the amino acid sequence of 215 residues for horse mackerel cathepsin B was obtained by RT-PCR and cloned. The deduced amino acid sequence contains a part of light and heavy chains of cathepsin B. The active sites and an N-glycosylation site were conserved across species. We also confirmed that the modori phenomenon was avoided by CA-074, a specific inhibitor for cathepsin B. Therefore, our results suggest that natural cysteine protease inhibitor(s), such as oryzacystatin derived from rice, can apply to thermal-gel processing of horse mackerel to avoid the modori phenomenon. Meanwhile, this endogenous protease may be used for food processing, such as weaning meal and food for the elderly. View Full-Text
Keywords: cathepsin B; endogenous protease; horse mackerel; food processing cathepsin B; endogenous protease; horse mackerel; food processing
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Yoshida, A.; Ohta, M.; Kuwahara, K.; Cao, M.-J.; Hara, K.; Osatomi, K. Purification and Characterization of Cathepsin B from the Muscle of Horse Mackerel Trachurus japonicus. Mar. Drugs 2015, 13, 6550-6565.

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