Enzymatic modification of sesame seed protein, sourced from waste resource for nutraceutical application

•Successful recovery of nutritionally rich protein concentrates from waste product.•Subsequent hydrolysis of the protein concentrate improved functional properties.•Ultrafiltration results in efficient yield of short peptides, evinced by MALDI-TOF.•Potent ACE-inhibitory activity of these short pepti...

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Bibliographic Details
Published in:Food and bioproducts processing 2015-04, Vol.94, p.70-81
Main Authors: Chatterjee, Roshni, Dey, Tanmoy Kumar, Ghosh, Mahua, Dhar, Pubali
Format: Article
Language:English
Subjects:
Angiotensin converting enzyme (ACE) inhibitor
Antioxidant
Bioactive peptides
Foaming
Functional properties
Hydrolysates
Hydrolysis
Papain
Peptides
Proteins
Sesame protein hydrolysates
Sesamum
Solubility
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Summary:•Successful recovery of nutritionally rich protein concentrates from waste product.•Subsequent hydrolysis of the protein concentrate improved functional properties.•Ultrafiltration results in efficient yield of short peptides, evinced by MALDI-TOF.•Potent ACE-inhibitory activity of these short peptides confirmed its bioactivity. The functional characteristics which include protein solubility at different pH, emulsifying and foaming properties, degree of hydrolysis, molecular weight distribution, antioxidant and ACE inhibitory activity of sesame protein hydrolysates prepared with pepsin, papain and alcalase enzymes were evaluated. The rate of degree of hydrolysis was found to reach maximum (25–30%) within the first time fragment i.e 10min but 80% of hydrolysis was obtained in 120min with alcalase. SDS-PAGE of hydrolysates with papain, pepsin and alcalase evinced bands of low molecular weight protein of 14.3kDa and even lower for alcalase treatment of 120min. Hydrolysates so formed were of improved functional properties as evident from emulsifying and foaming property. Hydrolysis with different proteases enhanced the protein solubility significantly at pH 7.0. Antioxidative assay revealed radical scavenging activity of the hydrolysates with papain hydrolysates showing maximum antioxidative efficacy. The ultra-filtered peptide fractions which showed comparable ACE inhibitory activity were sequenced by MALDI-TOF and matched to that of previously identified ACE inhibitory peptides. The results corroborate the ACE inhibitory effect of the peptides. Hence, these highly bioactive protein hydrolysates produced from waste sesame meals can be successfully employed in various functional food formulations.
ISSN:0960-3085
1744-3571
DOI:10.1016/j.fbp.2015.01.007