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Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma)

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Title: Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma)
Authors: Kishimura, Hideki Browse this author →KAKEN DB
Klomklao, Sappasith Browse this author
Benjakul, Soottawat Browse this author
Chun, Byung-Soo Browse this author
Keywords: Walleye pollock
Theragra chalcogramma
Pyloric cecum
N-terminal amino acid sequence
Frigid zone fish
Issue Date: 1-Jan-2008
Publisher: Elsevier Ltd.
Journal Title: Food Chemistry
Volume: 106
Issue: 1
Start Page: 194
End Page: 199
Publisher DOI: 10.1016/j.foodchem.2007.05.056
PMID: 11470450
Abstract: Trypsin was purified from the pyloric ceca of walleye pollock (Theragra chalcogramma) by gel filtration on Sephacryl S-200 and Sephadex G-50. The final enzyme preparation was nearly homogeneous in sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS–PAGE) and the molecular mass of the enzyme was estimated to be 24 kDa by SDS–PAGE. Trypsin activity was effectively inhibited by serine protease inhibitors, such as soybean trypsin inhibitor and TLCK. Trypsin had maximal activities at around pH 8.0 and 50 °C for the hydrolysis of Nα-p-tosyl-l-arginine methyl ester hydrochloride. Trypsin was unstable above 30 °C and below pH 5.0, and was stabilized by calcium ions. Walleye pollock trypsin was more thermally unstable than trypsin from the Temperate Zone fish and Tropical Zone fish. The N-terminal amino acid sequence of the trypsin, IVGGYECTKHSQAHQVSLNS, was found, and the sequential identity between the walleye pollock trypsin and Frigid Zone fish trypsin was higher (85–100%) than with Temperate Zone fish trypsin (75–90%), Tropical Zone fish trypsin (75–85%), or mammalian trypsin (60–65%).
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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