THE EFFECT OF COOKING ON PROTEINS FROM ACHA (DIGITARIA-EXILIS) AND DURUM-WHEAT

被引:13
作者
JIDEANI, AI [1 ]
APENTEN, RKO [1 ]
MULLER, HG [1 ]
机构
[1] UNIV LEEDS,PROCTER DEPT FOOD SCI,LEEDS LS2 9JT,W YORKSHIRE,ENGLAND
关键词
ACHA PROTEINS; DURUM WHEAT; EXTRACTABILITY; IN-VITRO DIGESTIBILITY; ELECTROPHORESIS; AMINO ACID COMPOSITION; DIGITARIA PROTEINS;
D O I
10.1002/jsfa.2740650415
中图分类号
S [农业科学];
学科分类号
09 ;
摘要
The effect of cooking on proteins from acha and durum wheat was assessed from an analysis of protein extractability, gel electrophoretic profiles, in-vitro protein digestibility (IVPD) and the amino acid compositions of wholemeal flour and residue proteins. Heating wholemeal flour samples at 100-140 degrees C (t = 10-40 min) resulted in 0-30% and 45-55% decreases in acha and durum protein solubility, respectively. In general, high molecular weight (30-70 kDa) protein subunits were more susceptible to heat damage. For both cereals, sodium dodecyl sulphate (SDS; 10 g litre(-1)) and/or dithiothreitol (DTT; 10 mM) increased protein solubility in unheated and heated samples. The IVPD index was 90-91% and was not significantly altered by cooking (100-120 degrees C, t = 40 min). Cooking at extreme temperatures (140 degrees C, t = 40 min) reduced the IVPD by 8% (P = 0.05). Osborne fractionation resulted in a durum or acha residue level of 7.8% or 55.2%. Treatment with solvent containing propanol, SDS and/or DTT at room temperature followed by SDS-polyacrylamide gel electrophoresis of non-solubilised proteins showed that the glutelin fraction of acha, with the exception of a 65 kDa subunit, was insoluble owing to strong inter-subunit hydrophobic and disulphide interactions. Wholemeal acha flour and residue protein showed a significantly greater level of hydrophobic and sulphur amino acids as well as glutamine which is associated with H-bonding. The possibility that cereal protein solubility is also dependent on protein-carbohydrate links is discussed.
引用
收藏
页码:465 / 476
页数:12
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