Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): Isolation and characterization

Kishimura, Hideki; Tokuda, Yusuke; Yabe, Mamoru; Klomklao, Sappasith; Benjakul, Soottawat; Ando, Seiichi

Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): Isolation and characterization

Kishimura, Hideki; Tokuda, Yusuke; Yabe, Mamoru et al.

Food Chemistry, 2007, 100(4), 1490-1495

Permalink : https://hdl.handle.net/2115/14904

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アクセス権	open access
URI	https://hdl.handle.net/2115/14904
タイトル	Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii) and elkhorn sculpin (Alcichthys alcicornis): Isolation and characterization
著者	Kishimura, Hideki ; Tokuda, Yusuke ; Yabe, Mamoru ; Klomklao, Sappasith ; Benjakul, Soottawat ; Ando, Seiichi
e-Rad_Researcher 50204855 著者名 Kishimura, Hideki
著者名 Tokuda, Yusuke
e-Rad_Researcher 80174572 著者名 Yabe, Mamoru
著者名 Klomklao, Sappasith
著者名 Benjakul, Soottawat
著者名 Ando, Seiichi
言語	英語
キーワード	Jacopever
	Sebastes schlegelii
	Elkhorn sculpin
	Alcichthys alcicornis
	Pyloric ceca
	Trypsin
	Characteristics
発行日	2007
出版者	Elsevier B.V.
収録物名	Food Chemistry
巻(号)	100(4)
ページ	1490-1495
抄録	Trypsins from the pyloric ceca of jacopever (Sebastes schlegelii), TR-J, and elkhorn sculpin (Alcichthys alcicornis), TR-E, were purified by gel filtration on Sephacryl S-200 and Sephadex G-50. The molecular weights of TR-J and TR-E were estimated to be 24,000 Da by sodium dodecyl sulfate–polyacrylamide gel electrophoresis. TR-J and TR-E revealed optimum temperatures of 60 and 50 °C, respectively, and showed the same optimum pH (pH 8.0) for hydrolysis of Nα-p-tosyl-l-arginine methyl ester. TR-J and TR-E were unstable at above 50 and 40 °C, respectively, and were more stable at alkaline pH than at acidic pH. Thermal stabilities of TR-J and TR-E were highly calcium dependent. These purified trypsin enzymes were inhibited by serine protease inhibitors, such as TLCK and soybean trypsin inhibitor. The N-terminal amino acid sequences of TR-J and TR-E were also investigated. The N-terminal amino acid sequences of TR-J, IVGGYECKPYSQPHQVSLNS, and TR-E, IVGGYECTPHSQAHQVSLNS, were found, and these sequences showed highly homology to other fish trypsins.
資源タイプ	学術雑誌論文
出版タイプ	Accepted Manuscript
PISSN	0308-8146
関連情報	URI http://www.sciencedirect.com/science/journal/03088146
関連情報 (isVersionOf)	出版社版DOI https://doi.org/10.1016/j.foodchem.2005.11.040