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Surface Hydrophobicity and Protein Cross‐Linking in Rice Subjected to Varying Drying and Tempering Conditions
Author(s) -
Tang S.,
Hettiarachchy N.S.,
Ju Z.,
Cnossen A.
Publication year - 2002
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2002.tb08840.x
Subject(s) - glutelin , chemistry , cystine , food science , moisture , tempering , lysine , chromatography , storage protein , materials science , biochemistry , organic chemistry , amino acid , cysteine , composite material , gene , enzyme
Rough rice was subjected to 25 °C or 60 °C drying with or without 3 h of tempering at 16.9% relative humidity to obtain rice flours. Proteins extracted from these flours were evaluated for surface hydrophobicity, molecular size, and protein cross‐linking via lysine‐carbohydrate interaction and formation of S‐S bond. Drying at 60 °C significantly increased glutelin surface hydrophobicity ( P < 0.05), but did not affect moisture, protein, glutelin components and their molecular sizes, and cystine and available lysine contents in comparison with drying at 25 °C. Therefore, drying at 60 °C is considered ineffective to cause protein cross‐linking and glutelin changes in molecular size.