Transglutaminase-induced or citric acid-mediated cross-linking of whey proteins to tune the characteristics of subsequently desolvated sub-micron and nano-scaled particles. (November 2014)

• Record Type: Journal Article
• Authors: Bagheri, Leila; Yarmand, Mohammadsaeed; Madadlou, Ashkan; Mousavi, Mohammad E.
• Is Part Of: Journal of microencapsulation. Volume 31:Number 7(2014:Nov.)
• Page Start: 636
• Page End: 643
• Publication Date: 2014-11
• Subjects: Microencapsulation -- Periodicals; Controlled release technology -- Periodicals; 615.19
• DOI: 10.3109/02652048.2014.911377
• Languages: English
• ISSNs: 0265-2048

Abstract

<abstract> <title>Abstract</title> <p>Whey proteins were inter-connected either by the enzyme transglutaminase or citric acid and then desolvated with ethanol to generate particles. Both samples comprised of sub-micron (&gt;300 nm) and nano-scaled (∼100 nm) particles based on the hydrodynamic size measurements. Enzyme-induced cross-linking of proteins yielded more monodisperse particles and decreased the mean size of the major (nano-scaled) fraction of particles. Scanning electron microscopy images revealed a spherical morphology for all samples with mean sizes of &lt;40 nm. Atomic force microscopy indicated a lower height for the particles from enzymatically cross-linked proteins. The mediating role of citric acid in bridging the proteins was confirmed by Fourier transform infrared spectroscopy. Differential scanning calorimetry indicated that pre-heating of protein solution before cross-linking and desolvation denatured the proteins entirely. <italic>In vitro</italic> degradation of whey protein particles in a simulated gastric fluid demonstrated that cross-linking of whey proteins before desolvation stage enhanced significantly the digestion stability of particles.</p> </abstract>