Mitigation of antinutritional factors and protease inhibitors of defatted winged bean-seed proteins using thermal and hydrothermal treatments: Denaturation/unfolding coupled hydrolysis mechanism

Sami Saadi; Nazamid Saari; Hasanah Mohd Ghazali; Mohammed Sabo Abdulkarim

doi:10.1016/j.crfs.2022.01.011

Mitigation of antinutritional factors and protease inhibitors of defatted winged bean-seed proteins using thermal and hydrothermal treatments: Denaturation/unfolding coupled hydrolysis mechanism

Curr Res Food Sci. 2022 Jan 17:5:207-221. doi: 10.1016/j.crfs.2022.01.011. eCollection 2022.

Authors

Sami Saadi^{1

2}, Nazamid Saari², Hasanah Mohd Ghazali², Mohammed Sabo Abdulkarim³

Affiliations

¹ Institut de la Nutrition, de l'Alimentation et des Technologies Agro-alimentaires INATAA 25017, Université Frères Mentouri, Constantine 1, Algeria.
² Department of Food Science, Faculty of Food Science and Technology, Universiti Putra Malaysia, 43400, Serdang, Selangor, Malaysia.
³ Department of Microbiology and Biotechnology, Federal University Dutse, Nigeria.

Abstract

The inactivation of antinutritional factors, protease inhibitors within winged bean protein was induced by two respective method treatments. The physical method based on steam vapor that was conducted using an autoclave and chemical method consisting on pH-gradients of buffer solutions prepared at respective acidic pH, neutral pH and alkaline pH ranges. The activity of remaining protease inhibitors of bowman birk inhibitor (BBI), and kunitz-trypsin inhibitor (KTI) after and before treatments was enzymatically confirmed using relevant antagonistic trypsin and combined trypsin-α-chymotrypsin digests. The resulting molecular assembly indicating an interval molecular relaxation range of °0.16 < °DA < °0.2 corresponding to reconformation in protein units with volume-mass changes of -2.17 < ∂v' < +2.17 and with denaturation/unfolding efficiency based on heat capacity ΔCp of 36.36 < DE/UF% < 54.67. These structural changes had a great benefit in determining and producing functional protein hydrolysates.

Keywords: Competitive inhibitors; Denaturation/unfolding; Hydrolysis levels; Molecular assembly; Proteolysates; Transition energy.