Author ORCID Identifier:
Date of Graduation
12-2025
Document Type
Thesis
Degree Name
Master of Science in Food Science (MS)
Degree Level
Graduate
Department
Food Science
Advisor/Mentor
Rahman, Mahfuzur
Committee Member
Atungulu, Griffiths
Second Committee Member
Kariyat, Rupesh
Third Committee Member
Ferreira, Sun
Keywords
charge-based separation; plant-based cheese; protein functionality; protein particle charge; rice protein; tribo-electrostatic separation
Abstract
Abstract Rice milling generates large volumes of bran and broken kernels that are often underused despite being rich in protein. This work first compared proteins from brown rice, broken kernels, and rice bran of a single cultivar, then applied tribo-electrostatic dry fractionation to rice bran protein to further improve its quality. Rice bran contained the highest albumin fraction, whereas broken kernels were richer in glutelin subunits (10–50 kDa). Rice bran protein showed higher β-sheet and random coil structures, while brown rice protein exhibited greater solubility of 18.37%, lower surface hydrophobicity of 34.26, and higher oil-holding capacity of 163.79 g/100 g. Additionally, a higher proportion of essential amino acids and improved in vitro digestibility of 67.61%. Bran protein had higher surface hydrophobicity of 43.18, lower solubility of 13.31%, and greater water-holding capacity of 68.27 g/100 g, consistent with its elevated β-sheet content. When used in plant-based cheese, brown rice protein produced a firmer texture, broken kernel protein yielded softer, and rice bran protein reduced oil separation, favoring creamy applications. Tribo-electrostatic separation of RBP at different pH levels produced fractions with distinct net charges and functionalities. The greatest protein separation efficiency was achieved for RBP 9.5 fractions of 70.30%, with 49.88% recovery in the positively charged RBP 9.5 +. These fractions showed smaller, more dispersed particles, higher absolute ζ-potential, higher solubility, and greater oil-holding capacity. In contrast, RBP 2.0 − displayed strong aggregation, high surface hydrophobicity of 84.20, and low solubility of 17.20%. Together, these results highlight rice milling byproducts as versatile, sustainable protein sources, and tribo-electrostatic separation could tailor their functionality for diverse plant-based foods.
Citation
Galib, R. M. (2025). Rice Protein from Milling Side Streams: Wet and Dry Fractionation, Quality Evaluation, and Applications in Plant-Based Cheese. Graduate Theses and Dissertations Retrieved from https://scholarworks.uark.edu/etd/6055
