Bio-based Pickering emulsifier from mangosteen residues-derived sodium caseinate grafted spherical cellulose nanocrystals: Stability, rheological properties and microstructure studies

• Main Authors: Yahya, Mazlita, Sakti, Satya Candra Wibawa, Fahmi, Mochamad Zakki, Chuah, Cheng Hock, Lee, Hwei Voon
• Format: Article
• Published: Elsevier 2024
• Subjects: QD Chemistry
• Online Access: http://eprints.um.edu.my/44243/; https://doi.org/10.1016/j.ijbiomac.2023.128696

This study focuses on the preparation of mangosteen rind-derived nanocellulose via green ascorbic acid hydrolysis. Subsequently, milk protein-grafted nanocellulose particles were developed as a renewable Pickering emulsifier for water-oil stabilization. The stabilizing efficiency of modified nanocellulose (NC-S) at different caseinate (milk protein) concentrations (1.5, 3.0, and 4.0 % w/v) was tested in a water-in-oil emulsion (W/O ratio of 40:60). At a concentration 3.0 % w/v of caseinate (3.0NC-S), the emulsion exhibited a stronger network of adsorption between water, Pickering emulsifier, and oil. This resulted in reduced oil droplet flocculation, increased stability over a longer period, and favorable emulsifying properties, as depicted in the creaming index profile, oil droplet distribution, and rheology analysis. Since 3.0NC-S demonstrated the best colloidal stability, further focus will be placed on its microstructural properties, comparing them with those of mangosteen rind (MG), cellulose, and nanocellulose (NC-L). The XRD profile indicated that both NC-L and NC-S possessed a cellulose nanocrystal structure characterized as type I beta with a high crystallinity index above 60 %. Morphology investigation shown that the NC-L present in the spherical shape of particles with nanosized ranging at diameters of 11.27 +/- 0.50 nm and length 11.76 +/- 0.46 nm, while modified NC-S showed increase sized at 14.26 +/- 4.60 nm and length 14.96 +/- 4.94 nm. The increment of particle sizes from NC-L to NC-S indicated 2.82 x 10-15 mg/m2 of surface protein coverage by caseinate functional groups.