Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma)
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 enzy...
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Online Access: | http://hdl.handle.net/2115/30273 https://doi.org/10.1016/j.foodchem.2007.05.056 |
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fthokunivhus:oai:eprints.lib.hokudai.ac.jp:2115/30273 2023-05-15T18:32:50+02:00 Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma) Kishimura, Hideki Klomklao, Sappasith Benjakul, Soottawat Chun, Byung-Soo http://hdl.handle.net/2115/30273 https://doi.org/10.1016/j.foodchem.2007.05.056 eng eng Elsevier Ltd. http://www.sciencedirect.com/science/journal/03088146 http://hdl.handle.net/2115/30273 Food Chemistry, 106(1): 194-199 http://dx.doi.org/10.1016/j.foodchem.2007.05.056 Walleye pollock Theragra chalcogramma Pyloric cecum Trypsin N-terminal amino acid sequence Thermostability Frigid zone fish 487.78 article (author version) fthokunivhus https://doi.org/10.1016/j.foodchem.2007.05.056 2022-11-18T01:01:34Z 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%). Article in Journal/Newspaper Theragra chalcogramma Hokkaido University Collection of Scholarly and Academic Papers (HUSCAP) Food Chemistry 106 1 194 199 |
institution |
Open Polar |
collection |
Hokkaido University Collection of Scholarly and Academic Papers (HUSCAP) |
op_collection_id |
fthokunivhus |
language |
English |
topic |
Walleye pollock Theragra chalcogramma Pyloric cecum Trypsin N-terminal amino acid sequence Thermostability Frigid zone fish 487.78 |
spellingShingle |
Walleye pollock Theragra chalcogramma Pyloric cecum Trypsin N-terminal amino acid sequence Thermostability Frigid zone fish 487.78 Kishimura, Hideki Klomklao, Sappasith Benjakul, Soottawat Chun, Byung-Soo Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma) |
topic_facet |
Walleye pollock Theragra chalcogramma Pyloric cecum Trypsin N-terminal amino acid sequence Thermostability Frigid zone fish 487.78 |
description |
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%). |
format |
Article in Journal/Newspaper |
author |
Kishimura, Hideki Klomklao, Sappasith Benjakul, Soottawat Chun, Byung-Soo |
author_facet |
Kishimura, Hideki Klomklao, Sappasith Benjakul, Soottawat Chun, Byung-Soo |
author_sort |
Kishimura, Hideki |
title |
Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma) |
title_short |
Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma) |
title_full |
Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma) |
title_fullStr |
Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma) |
title_full_unstemmed |
Characteristics of trypsin from the pyloric ceca of walleye pollock (Theragra chalcogramma) |
title_sort |
characteristics of trypsin from the pyloric ceca of walleye pollock (theragra chalcogramma) |
publisher |
Elsevier Ltd. |
url |
http://hdl.handle.net/2115/30273 https://doi.org/10.1016/j.foodchem.2007.05.056 |
genre |
Theragra chalcogramma |
genre_facet |
Theragra chalcogramma |
op_relation |
http://www.sciencedirect.com/science/journal/03088146 http://hdl.handle.net/2115/30273 Food Chemistry, 106(1): 194-199 http://dx.doi.org/10.1016/j.foodchem.2007.05.056 |
op_doi |
https://doi.org/10.1016/j.foodchem.2007.05.056 |
container_title |
Food Chemistry |
container_volume |
106 |
container_issue |
1 |
container_start_page |
194 |
op_container_end_page |
199 |
_version_ |
1766217027651895296 |