Decrease of the Soybean Glycinin Digestibility in Excess Denaturation; Effect of Refolding
- 1 June 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in Agricultural and Biological Chemistry
- Vol. 43 (6) , 1219-1223
- https://doi.org/10.1080/00021369.1979.10863611
Abstract
The digestibility of denatured glycinin with various denaturants such as urea, GuHCl [guanidine hydrochloride] and SDS [sodium dodecyl sulfate], and heat treatment, was studied by a pH -stat method. It increases with increasing concentration of the denaturants and heating temperature. Further addition of the denaturants and 120.degree. C heating caused a decrease of digestibility. In urea denaturation, optical measurements indicate that conformation of the protein appreciably refolds after the removal of the denaturant. Gel filtration analyses also indicate the partial refolding of the structure of the protein. The refolding of the protein may play an important role in the decrease of the digestibility. Structural differences of denatured glycinin from the native one and reasons for the decrease of the digestibility cannot be revealed yet.This publication has 6 references indexed in Scilit:
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