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KMID : 1007520000090060341
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Food Science and Biotechnology
2000 Volume.9 No. 6 p.341 ~ p.345
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Effects of Hydroquinone on Wheat Gluten Extrusion
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Koh Bong-Kyung
Lim Seung-Taik
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Abstract
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To investigate the role of protein cross-linking of the extruded wheat flour, vital wheat gluten was extruded as a model system of the wheat flour fraction and reducing reagent, hydroquinone (2% dry gluten weight) was added to inhibit the protein cross-link formation during extrusion. Physical shapes of the extruded gluten without starch showed protein aggregates with no puffing, rough surface and the micro structure showing a typical fibrous protein structure. Hydroquinone addition produced more irregular shapes and a little puffed short pieces of the gluten extrudates and accelerated cell breakdown which results in broken and rough surface cell instead of the fibrous structure of gluten. In comparison to the unextruded vital wheat gluten, extruded gluten was increased the water absorption capacity, decreased sulfur and nitrogen contents and decreased protein solubility without reduction of disulfide bonds. Protein solubility of the denatured gluten extrudates with hydroquinoe was increased, while the organic materials containing nitrogen was decreased. The most notable point about the extruded gluten´s amino acid compositions was the low level of proline which was broken by high temperature short time extrusion processing. Decrease of sulfur-containing amino acids was mainly observed from cysteine rather than methionine. However, inhibition of protein cross-link formation with hydroquinone did not show major effect on the amino acid composition of gluten. Above results suggests that protein cross-link is an important characteristic fibrous structure of the extruded gluten accompanied with changes of amino acid composition due to proline and cysteine.
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