Structural properties of trypsin from cold-adapted fish,arabesque greenling (<Emphasis Type="Italic">Pleurogrammus azonus</Emphasis>) |
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Authors: | Gaku Kanno Hideki Kishimura Seiichi Ando Sappasith Klomklao Sitthipong Nalinanon Soottawat Benjakul Byung-Soo Chun Hiroki Saeki |
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Affiliation: | (1) Laboratory of Marine Products and Food Science, Research Faculty of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido 041-8611, Japan;(2) Faculty of Fisheries, Kagoshima University, Shimoarata, Kagoshima 890-0056, Japan;(3) Department of Food Science and Technology, Faculty of Technology and Community Development, Thaksin University, Phattalung Campus, Phattalung, 93110, Thailand;(4) Department of Food Technology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, 90112, Thailand;(5) Faculty of Food Science and Biotechnology, Pukyong National University, Busan, 608-737, Republic of Korea; |
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Abstract: | A cDNA clone encoding trypsin (AG-T) was isolated from the pyloric ceca of cold-adapted fish, arabesque greenling (Pleurogrammus azonus). The cDNA was composed of 892 bp with an open reading frame of 729 bp at nucleotide positions 25–753. Similar to all the
known trypsin, the AG-T seemed to be synthesized as preproenzyme that contains a hydrophobic signal peptide, an activation
pentapeptide and a mature trypsin of 222 amino acid residues. The AG-T also completely conserved the major structural features
common to trypsin such as the catalytic triad (His57, Asp102, and Ser195), the obligatory Asp189 and twelve Cys residues.
On the other hand, the AG-T possessed the deletion of Tyr151 and substitution of Pro152 for Gly in the autolysis loop when
aligned with the sequence of tropical-zone fish and bovine trypsins. In addition, Val75 concerned in a combination with calcium
ion was exchanged for Ala in the AG-T, and the content of positively charged amino acid residues at the calcium-binding site
of the AG-T was three times higher than those of tropical-zone fish trypsins. Moreover, the ratio between charged and hydrophobic
amino acid residues in the N-terminal region of the AG-T was also higher than those of temperate-zone fish and tropical-zone fish trypsins. Such structural
properties of the AG-T would contribute to its low thermostability. |
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