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Impact of processing conditions on the extractability and molecular weight distribution of proteins in parboiled brown rice

Author:
Buggenhout, Joke, Brijs, Kristof, Delcour, Jan A.
Source:
Journal of cereal science 2013 v.58 no.1 pp. 8-14
ISSN:
0733-5210
Subject:
albumins, brown rice, disulfide bonds, dithiothreitol, globulins, glutelins, hot water treatment, hydrogen bonding, hydrophobic bonding, liquid chromatography, molecular weight, nutritive value, pH, paddies, parboiling, polymerization, prolamins, soaking, sodium dodecyl sulfate, sodium phosphate, steaming, texture, urea
Abstract:
Parboiling, a hydrothermal treatment of paddy or brown rice, impacts the texture and nutritional characteristics of cooked rice. We investigated the impact of parboiling conditions on the extractability and molecular weight (MW) distribution of proteins in brown rice. Brown rice was parboiled using different soaking and steaming conditions. The extractability and MW distribution of proteins extracted with sodium phosphate buffer (50 mmol/L; pH 6.8) containing (i) 2.0% sodium dodecyl sulfate (SDS), (ii) 2.0% SDS/1.0% dithiothreitol (DTT)/6.0 mol/L urea, (iii) 2.0% SDS/1.0% DTT, and (iv) 2.0% SDS/6.0 mol/L urea was examined by size exclusion-high performance liquid chromatography. Depending on the parboiling conditions, protein extractabilities in media (i), (ii), (iii), and (iv) ranged from 14 to 25%, 83 to 100%, 40 to 82%, and 19 to 37%, respectively. Unlike soaking conditions, steaming conditions had pronounced effects on the level of extractable protein. In general, more severe steaming conditions caused greater reductions in protein extractability, indicating a denser protein network. Apparent MW profiles revealed that especially glutelins polymerize upon severe steaming. Albumins, globulins and prolamins either polymerize through disulfide bonds and/or interact with one another through hydrogen bonds or hydrophobic interactions to form a separate protein network or become incorporated in the glutelin network.
Agid:
1128560