Abstract

Protein-polysaccharide covalent complexes exhibit better physicochemical and functional properties than single protein or polysaccharide. To promote the formation of the covalent complex from lactoferrin (LF) and beet pectin (BP), we enhanced the Maillard reaction between LF and BP by using an ultrasound-assisted treatment and studied the structure and functional properties of the resulting product. The reaction conditions were optimized by an orthogonal experimental design, and the highest grafting degree of 55.36% was obtained by ultrasonic treatment at 300 W for 20 min and at LF concentration of 20 g/L and BP concentration of 9 g/L. The formation of LF-BP conjugates was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FTIR) spectroscopy. Ultrasound-assisted treatment can increase the surface hydrophobicity, browning index, 1,1-diphenyl-2-picryl-hydrazyl (DPPH) and 2,2’-azinobis-(3-ethylbenzthiazoline-6-sulphonate) (ABTS) free radicals scavenging activity of LF due to the changes in the spatial configuration and formation of Maillard reaction products. The thermal stability, antioxidant activity and emulsifying property of LF were significantly improved after combining with BP. These findings reveal the potential application of modified proteins by ultrasonic and heat treatment.

Highlights

  • Lactoferrin (LF), a member of the transferrin family, is an 80 kDa iron-binding glycoprotein added into nutritional supplements, infant formula, cosmetics and toothpaste [1]

  • The residual amount of C-LF-beet pectin (BP) was higher than those of dry-heating treated and physically-mixed LF and BP, while dry-heated LF-BP (D-LF-BP) did not show much increment compared to mixture of untreated LF-BP (M-LF-BP). These results further prove the occurrence of Maillard reaction and the better effect of ultrasound-assisted treatment on Maillard reaction than that of dry-heating treatment

  • Ultrasound-assisted treatment significantly enhances the covalent binding between LF and BP

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Summary

Introduction

Lactoferrin (LF), a member of the transferrin family, is an 80 kDa iron-binding glycoprotein added into nutritional supplements, infant formula, cosmetics and toothpaste [1]. LF has many advantages such as antimicrobial, antibacterial, antitumor and anti-inflammation activities and is often used as an emulsifier or essential component and as an amphiphilic milk protein in various delivery systems [2]. Chemical, physical and enzymatic modifications are widely used to improve the functional properties of food proteins. The majority of chemical modifications of food proteins can cause health problem in some way, while enzymatic modifications are more expensive. A food-derived reaction that mostly happens between proteins and polysaccharides, performs without any extra chemical reagent and is widely used in protein modification [4]. The conjugation of proteins with polysaccharide is an efficient way to improve their functions, such as emulsibility, gel, and foaming properties [5]

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