Elsevier

Ultrasonics Sonochemistry

Volume 43, May 2018, Pages 227-236
Ultrasonics Sonochemistry

Changes in structure and antioxidant activity of β-lactoglobulin by ultrasound and enzymatic treatment

https://doi.org/10.1016/j.ultsonch.2018.01.017Get rights and content
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Highlights

  • UAE treatment considerable impact on the structure and antioxidant activity of β-Lg.

  • HIU increased the proteolysis of β-Lg by both pepsin and trypsin.

  • The antioxidative activity of β-Lg and its hydrolyzed fragments was compared.

  • UAE treated β-Lg exhibited significant oxygen scavenging activity in Caco-2cells.

Abstract

Effects of ultrasound (20–40% amplitudes at 45–55 °C) and enzymatic (pepsin and trypsin) treatment on structure and antioxidant activity of β-lactoglobulin were studied. Changes in structure of β-lactoglobulin were investigated using spectroscopy techniques and changes in antioxidant activity were measured by chemical and cellular-based assays. Ultrasound treatment had considerable impact on the structure of β-lactoglobulin and increased the susceptibility of β-lactoglobulin to both pepsin and trypsin proteolysis. Intrinsic fluorescence intensity of β-lactoglobulin was increased by ultrasound and then decreased after following enzymatic treatment. Compared with control, the β-lactoglobulin after ultrasound and enzymatic treatments showed significantly higher oxygen scavenging activities in Caco-2 cells models, ABTS (2, 2′-Azinobis-3-ethylbenzthiazoline-6-sulphonate) radical scavenging activity and oxygen radical absorbance capacity (p < 0.05). Results indicated that ultrasound treatment increased the proteolysis of β-lactoglobulin by both pepsin and trypsin and improved the antioxidant activity of the protein and its proteolytic products.

Keywords

β-Lactoglobulin
Ultrasound treatment
Proteolysis
Antioxidant activity

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