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J Sci Food Agric ; 102(5): 1903-1911, 2022 Mar 30.
Article in English | MEDLINE | ID: mdl-34516659

ABSTRACT

BACKGROUND: Kafirin is a prolamin protein located in the corneous endosperm of sorghum. The conventional thermal processing of kafirin reduces its solubility, which limits its utilization in the food industry. Therefore, the study was aimed to investigate the effect of in situ thermal modification of kafirin using two different electromagnetic thermal treatments, namely infrared (IR) and microwave (MW) radiation, on the physicochemical, structural, thermal, and antioxidant properties. RESULTS: The results demonstrated that both the thermal modifications improved yield, purity, and solubility of the kafirin with a decrease in hydrophobicity. However, IR-treated samples showed higher solubility (910.67 g kg-1 ) and lower hydrophobicity (387.67). The IR modifications also improved the ratio of α helix/ß sheets to a great extent. The alterations in the disulfide content were concomitant with the improvement in the thermal stability of kafirin. Sodium dodecyl sulfate polyacrylamide gel electrophoresis showed variations in the band intensities of ß- and γ-kafirin, indicating alterations in the kafirin subunits. Morphological examination of kafirin revealed surface withering and agglomeration. Notably, IR treatment improved the antioxidant activity more efficiently (from 32.11% to 74.05%). CONCLUSION: Although both the IR and MW treatments modified kafirin, the effect seemed to be more pronounced in IR modification. The IR-modified kafirin had better solubility and lesser hydrophobicity than MW-modified kafirin. The physicochemical and structural changes induced by IR treatment improved the biological activity of kafirin, in terms of antioxidant activity. Therefore, it was concluded that the in situ IR modification of kafirin can alter its characteristic properties, improving its potential as a food ingredient. © 2021 Society of Chemical Industry.


Subject(s)
Infrared Rays , Microwaves , Plant Proteins , Plant Proteins/chemistry , Plant Proteins/radiation effects , Prolamins/chemistry , Prolamins/radiation effects , Protein Conformation , Solubility
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