HUSCAP logo Hokkaido Univ. logo

Hokkaido University Collection of Scholarly and Academic Papers >
Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences >
Peer-reviewed Journal Articles, etc >

A thermostable trypsin from freshwater fish Japanese dace (Tribolodon hakonensis) : a comparison of the primary structures among fish trypsins

Files in This Item:
FishPhysiolBiochem_2019-45-561.pdf808.22 kBPDFView/Open
Please use this identifier to cite or link to this item:http://hdl.handle.net/2115/77217

Title: A thermostable trypsin from freshwater fish Japanese dace (Tribolodon hakonensis) : a comparison of the primary structures among fish trypsins
Authors: Kanno, Gaku Browse this author
Klomklao, Sappasith Browse this author
Kumagai, Yuya Browse this author →KAKEN DB
Kishimura, Hideki Browse this author →KAKEN DB
Keywords: Freshwater fish
Japanese dace
Primary structure
Thermostability
Tribolodon hakonensis
Trypsin
Issue Date: Apr-2019
Publisher: Springer
Journal Title: Fish physiology and biochemistry
Volume: 45
Issue: 2
Start Page: 561
End Page: 571
Publisher DOI: 10.1007/s10695-018-0600-3
Abstract: Trypsin from Japanese dace (Tribolodon hakonensis) (JD-T) living in freshwater (2-18 degrees C) was purified. JD-T represented typical fish trypsin characteristics regarding the effects of protease inhibitor, calcium-ion, and pH. For the effect of temperature, JD-T quite resembled to the trypsins from tropical-zone marine fish and freshwater fish (the catfish cultured in Thailand), i.e., the optimum temperature was 60 degrees C, and it was stable below 60 degrees C at pH 8.0 for 15min incubation. From the data, it seemed that the trypsin from freshwater fish is thermostable in spite of the fact that their habitat temperatures are low. So, we determined the primary structure of JD-T to discuss its thermostability-structure relationship. JD-T possessed basic structural features of fish trypsin such as the catalytic triad, the Asp189 residue for substrate specificity, 12 Cys residues forming six disulfide-bridges, and the calcium-ion-binding loop. On the other hand, the contents of charged amino acid residues in whole JD-T molecule (16.2%) and N-terminal region (13.8%) were similar to those of tropical-zone marine fish and other freshwater fish trypsins. Then, JD-T conserved the five amino acid residues (Glu70, Asn72, Val75, Glu77, and Glu80) coordinate with calcium-ion, and the proportion of negatively charged amino acids to charged amino acids in the calcium-ion-binding region of JD-T (75.0%) was equivalent to those of tropical-zone marine fish and freshwater fish trypsins. Therefore, it was suggested that the high thermostability of JD-T are stemmed from these structural specificities.
Rights: The final publication is available at Springer via https://doi.org/10.1007/s10695-018-0600-3
Type: article (author version)
URI: http://hdl.handle.net/2115/77217
Appears in Collections:水産科学院・水産科学研究院 (Graduate School of Fisheries Sciences / Faculty of Fisheries Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 岸村 栄毅

Export metadata:

OAI-PMH ( junii2 , jpcoar )

MathJax is now OFF:


 

 - Hokkaido University