Enzymological characteristics of pepsinogens and pepsins purified from lizardfish (Saurida micropectoralis) stomach.

Autor: Kuepethkaew S; Biotechnology Program, Faculty of Agro and Bio Industry, Thaksin University, Phatthalung Campus, Pa-Phayom, Phatthalung 93210, Thailand., Zhang Y; Department of Food Science & Agricultural Chemistry, McGill University, 21111 Lakeshore Road, Ste-Anne-de-Bellevue, QC, H9X 3V9, Canada. Electronic address: yi.zhang10@mcgill.ca., Kishimura H; Laboratory of Marine Chemical Resource Science Development, Faculty of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, 041-8611, Japan., Kumagai Y; Laboratory of Marine Chemical Resource Science Development, Faculty of Fisheries Sciences, Hokkaido University, Hakodate, Hokkaido, 041-8611, Japan., Simpson BK; Department of Food Science & Agricultural Chemistry, McGill University, 21111 Lakeshore Road, Ste-Anne-de-Bellevue, QC, H9X 3V9, Canada., Benjakul S; International Center of Excellence in Seafood Science and Innovation, Faculty of Agro-industry, Prince of Songkla University, Hat Yai, Songkhla 90110, Thailand., Damodaran S; Department of Food Science, University of Wisconsin-Madison, Madison, WI, 53706, United States., Klomklao S; Department of Food Science and Technology, Faculty of Agro and Bio Industry, Thaksin University, Phatthalung Campus, Pa-Phayom, Phatthalung 93210, Thailand. Electronic address: sappasith@tsu.ac.th.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2022 Jan 01; Vol. 366, pp. 130532. Date of Electronic Publication: 2021 Jul 05.
DOI: 10.1016/j.foodchem.2021.130532
Abstrakt: One major pepsinogen, PG-I, and two minor pepsinogens, PG-II and PG-III were purified from lizardfish stomach by ammonium sulfate precipitation and two chromatographic columns. The three purified PGs migrated as single bands in native-PAGE gels with molecular weights (MW) ranging from 36 to 38 kDa. Each PG was converted to pepsin (P) at pH 2.0, and the MW were determined as 32 kDa (for P-I), 31 kDa (for P-II) and 30 kDa (for P-III). The optimum pH and temperature of pepsins were 2.0-3.5, and 40-50 °C. All 3 pepsins were strongly inhibited by pepstatin A. Divalent cations slightly stimulated the pepsin activities, but ATP had no effect on the pepsins. Purified pepsins were effective in the hydrolysis of various proteins. K m and k cat of the three pepsins for hemoglobin hydrolysis were 107.64-276.61 µM and 18.30-32.68 s -1 , respectively. The new pepsins have potential for use in protein food procession and modification.
(Copyright © 2021 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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