Electrophoresis to determine the molecular weight distribution in soluble proteins from various foods and their rumen-resistant residues in cattle
2001
Chaudhry, A.S. | Webster, A.J.F.
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 66 kDa. Low-MW (<25 kDa) peptides were greater in number than high-MW (>25 kDa) 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 0.12 RU; 29%) than their high-MW counterparts (0.12 RM vs 0.02 RU; 21%). In contrast, high-MW glutalin 1 was more resistant (0.03 RM vs 0.22 RU) than low-MW glutalin 1 (0.09 RM vs 0.26 RU) in most agricultural foods. Globulins contained the least and glutalins the most resistant peptides in distillers' foods. While this study reveals an association between dg, 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.
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