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Cold-adapted structural properties of trypsins from walleye pollock (Theragra chalcogramma) and Arctic cod (Boreogadus saida)

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Title: Cold-adapted structural properties of trypsins from walleye pollock (Theragra chalcogramma) and Arctic cod (Boreogadus saida)
Authors: Kanno, Gaku Browse this author
Kishimura, Hideki Browse this author →KAKEN DB
Yamamoto, Jun Browse this author →KAKEN DB
Ando, Seiichi Browse this author
Shimizu, Takeshi Browse this author
Benjakul, Soottawat Browse this author
Klomklao, Sappasith Browse this author
Nalinanon, Sitthipong Browse this author
Chun, Byung-Soo Browse this author
Saeki, Hiroki Browse this author →KAKEN DB
Keywords: Trypsin
Walleye pollock
Theragra chalcogramma
Arctic cod
Boreogadus saida
cDNA cloning
Primary structure
Cold adaptation
Issue Date: Dec-2011
Publisher: Springer-Verlag
Journal Title: European Food Research and Technology
Volume: 233
Issue: 6
Start Page: 963
End Page: 972
Publisher DOI: 10.1007/s00217-011-1592-8
Abstract: Complementary DNA clones encoding trypsins were isolated from pyloric ceca of cold-adapted fish, walleye pollock (Theragra chalcogramma) (WP-T) and Arctic cod (Boreogadus saida) (AC-T). The isolated full-length cDNA clones of WP-T and AC-T were 852 bp and 860 bp, respectively, and both cDNAs were contained an open reading frame of 726 bp. WP-T and AC-T seemed to be synthesized as preproenzyme that contains a signal peptide, an activation peptide, and a mature trypsin. Although the amino acid sequence identities of WP-T and AC-T to that of bovine trypsin were 64% and 63%, respectively, they completely conserved the structural features for catalytic function of trypsin. On the other hand, WP-T and AC-T possessed the four Met residues (Met135, Met145, Met175 and Met242) in their molecules and the deletion of Tyr151 and substitution of Pro152 for Gly in their autolysis loops when aligned with the sequences of tropical-zone fish and bovine trypsins. In addition, the contents of charged amino acid residues at the N-terminal regions (positions 20-50) of WP-T and AC-T were extremely higher than those of other fish and bovine trypsins. Moreover, one amino acid (Asn72) and two amino acids (Asn72 and Val75) coordinating with Ca2+ in bovine trypsin were exchanged for another amino acids in WP-T (His) and AC-T (His and Glu), respectively, and the contents of negative charged amino acids at their Ca^[2+]-binding regions were lower than those of tropical-zone fish and bovine trypsins. Therefore, it was considered that these structural characteristics of WP-T and AC-T are closely related to their lower thermo stability.
Rights: The original publication is available at
Type: article (author version)
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

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