TY - JOUR
T1 - Enzymological characteristics of pepsinogens and pepsins purified from lizardfish (Saurida micropectoralis) stomach
AU - Kuepethkaew, Sakonwat
AU - Zhang, Yi
AU - Kishimura, Hideki
AU - Kumagai, Yuya
AU - Simpson, Benjamin K.
AU - Benjakul, Soottawat
AU - Damodaran, Srinivasan
AU - Klomklao, Sappasith
N1 - Funding Information:
This work was supported by the National Research Council of Thailand as of fiscal year 2021 and the Thailand Science Research and Innovation (TSRI) under the Research and Researchers for Industries (RRI) to Sakonwat Kuepethkaew (PHD60I0088). The National Research Council of Thailand and Thaksin University for Project No. NRCI5-RSA63005 are also acknowledged.
Publisher Copyright:
© 2021 Elsevier Ltd
PY - 2022/1/1
Y1 - 2022/1/1
N2 - 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. Km and kcat 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.
AB - 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. Km and kcat 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.
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U2 - 10.1016/j.foodchem.2021.130532
DO - 10.1016/j.foodchem.2021.130532
M3 - Article
C2 - 34274702
AN - SCOPUS:85110199891
SN - 0308-8146
VL - 366
JO - Food Chemistry
JF - Food Chemistry
M1 - 130532
ER -