Lookup NU author(s): Dr Abdul Chaudhry
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Electrophoresis was used to visually identify and determine the molecular weight (MW) distribution of rumen-degradable and rumen-resistant or escape peptides in soluble proteins from 12 agricultural and distillers' food raw materials (RM) and their residues (RU) following 18h of in sacco rumen incubation (dg18) in cattle. Soluble proteins were extracted by using water, salt, acid and alkali in succession to represent albumins, globulins, glutalin 1 and glutalin 2 respectively. RM and RU differed substantially in the MW range, number and intensity of bands for various soluble proteins. The bands were mostly below the MW range of 66kDa. Low-MW (<25kDa) peptides were greater in number than high-MW (>25kDa) peptides in almost all soluble proteins from RM. Individual peptides behaved differently during rumen incubation. Their resistance to or escape from rumen degradation varied with the class of food, type of soluble protein and their MW range. On average, low-MW albumins in agricultural foods were more resistant to rumen degradation (0.41 RM vs 0.12RU; 29%) than their high-MW counterparts (0.12 RM vs 0.02RU; 21%). In contrast, high-MW glutalin 1 was more resistant (0.03RM vs 0.22RU) than low-MW glutalin 1 (0.09RM vs 0.26RU) in most agricultural foods. Globulins contained the least and glutalins the most resistant peptides in distillers' foods. While this study reveals an association between dg18 and protein type, structure and size, we do not recommend the immediate use of electrophoresis for routine food evaluation unless more studies are undertaken. It may, however, be suitable for further characterisation of the degradation of specific, selected peptides by specific micro-organisms. © 2001 Society of Chemical Industry.
Author(s): Chaudhry AS; Webster AJF
Publication type: Article
Publication status: Published
Journal: Journal of the Science of Food and Agriculture
ISSN (print): 0022-5142
ISSN (electronic): 1097-0010
Publisher: John Wiley & Sons Ltd
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