Characterisation and use of β-lactoglobulin fibrils for microencapsulation of lipophilic ingredients and oxidative stability thereof

Abstract

a b s t r a c tThere is a growing interest in using fibrils from food grade protein, e.g. b-lactoglobulin, as functional ingredients. In the present study, the functionality of fibrillar b-lactoglobulin from whey protein isolate (WPI) was compared to native WPI in terms of interfacial dilatational rheology and emulsifying activity at acidic conditions (pH 2.0 and 3.0). We report here for the first time data on microencapsulation of fish oil by spray-drying as well as oxidative stability of the oil in emulsions and microcapsules in dependence of WPI conformation. WPI fibrils exerted a significantly higher elasticity at the oil-water (o/w) interface and a better emulsifying activity at a fixed oil content compared to native WPI. Microencapsulation efficiency was also higher with fibrillar WPI (>95%) compared to native WPI ($90%) at pH 2.0 and a total oil and protein content of 40% and 2.2%, respectively, in the final powder. The oxidative deterioration was lower in emulsions and microcapsules prepared with fibrillar than with native WPI. This was attributed to improved interfacial barrier properties provided by fibrils and antioxidative effects of coexisting unconverted monomers, particularly hydrophilic peptides.

Food-grade micro-encapsulation systems that may induce satiety via delayed lipolysis: A review

“…The fibril length depends on reaction-time and shear rate (Akkermans et al 2008), and they have been used to reinforce microcapsules (Kroes-Nijboer et al 2012, Rossier-Miranda et al 2010. Recently, β-LG fibrils were found not only to provide a more elastic interface compared to native β-LG, but also a better oxidative stability to encapsulated fish oil core (Serfert et al 2014). At the same time it should be mentioned that some concerns exist regarding the potential toxicity of protein fibrils because these nanostructures might relate to protein misfolding diseases (e.g., CJD, Alzheimer's, Parkinson's and Huntington's diseases) (Raynes et al 2014).…”

Whey Protein Complexes with Green Tea Polyphenols: Antimicrobial, Osteoblast-Stimulatory, and Antioxidant Activities

“…WPI (BiPRO, Davisco Foods Int., Inc., Eden Prairie, MN, USA) with 97.7% protein and 75% bLG in dry matter (according to specification) was used as previously described [Serfert et al, 2014;Keppler et al, 2017]. GTE, > 95% (obtained from green tea leaves, catechins content > 75%, EGCG > 65%; according to specification) was purchased from Oskar Tropitzsch e. K. (Marktredwitz, Germany).…”

Negatively charged tangential flow ultrafiltration membranes for whey protein concentration

“…Whey proteins are known to be among the most nutritionally complete proteins and each individual whey protein has unique health benefits. The uses and properties of whey proteins may be found elsewhere [1][2][3][4]. Sweet whey contains about 5% lactose, 1% nonprotein nitrogen (NPN) and other small molecules like cheese color, minerals, and riboflavin (which imparts the yellow color to whey), 0.06-0.1% fat, and 0.6% protein.…”

“…The remainder is water. Thus, on a dry basis, whey contains about 10-12% protein that individually range in molecular mass from 8.6 kDa to 150 kDa [1,3]. The purpose of whey protein concentration is to increase the protein-to-dry-solids content from about 12% to 80% by removing water and the other small molecules while retaining protein.…”