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Improving the enzymolysis efficiency of lupin protein by ultrasound pretreatment: Effect on antihypertensive, antidiabetic and antioxidant activities of the hydrolysates

•The first study about the impact of ultrasound pretreatment (UP) on bioactivity of LPH.•MALDI-TOF-MS confirmed the UP effect on the molecular weight of LPH.•ACE inhibitory and antioxidant activities significantly increased after UP.•UP improved α-glucosidase and α-amylase inhibitory activities.•Bio...

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Published in:Food chemistry 2022-07, Vol.383, p.132457-132457, Article 132457
Main Authors: Fadimu, Gbemisola J., Gill, Harsharn, Farahnaky, Asgar, Truong, Tuyen
Format: Article
Language:English
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Summary:•The first study about the impact of ultrasound pretreatment (UP) on bioactivity of LPH.•MALDI-TOF-MS confirmed the UP effect on the molecular weight of LPH.•ACE inhibitory and antioxidant activities significantly increased after UP.•UP improved α-glucosidase and α-amylase inhibitory activities.•Bioactivity enhancement was dependent on protease type and sonication time. This study evaluated the impact of ultrasound pretreatment (UP) and enzyme type (flavourzyme, alcalase) on amino acid composition, antihypertensive, antidiabetic, and antioxidant activities of lupin protein hydrolysate (LPH). The UP altered molecular weight of the hydrolysates as revealed by SDS-PAGE and MALDI-TOF and their surface hydrophobicity and thermal stability. Amino acid analysis revealed that glutamic acid, aspartic acid, arginine, and leucine were the dominant amino acids lupin protein. Generally, sonicated hydrolysates exhibited higher biological activity than non-sonicated samples and the original LPI. Alcalase hydrolysate pretreated for 10 min showed the highest DPPH and metal chelating activities. Highest ACE inhibitory activity was observed in flavourzyme hydrolysate after 5 min of UP, while maximum α-amylase and glucosidase inhibitory activity was achieved after 10 min of UP in flavourzyme hydrolysate. The results obtained in this study demonstrated the potentials of UP as a valuable tool for enhancing the biological activity of lupin proteins.
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2022.132457