Proanthocyanidins Modulate Rumen Enzyme Activities and Protein Utilization In Vitro

This study investigated the principal leaf protein (rubisco) solubilization and in vitro ruminal enzyme activity in relation to the molecular structure of proanthocyanidins extracted from leaves of Anogeissus pendula and Eugenia jambolana. Six proanthocyanidin fractions were extracted by 50% (v/v) methanol&ndash:water followed by 70% (v/v) acetone&ndash:water and then distilled water from leaves of A. pendula (AP) and E. jambolana (EJ) to yield EJ&ndash:70, EJ&ndash:50, EJ&ndash:DW, AP&ndash:70, AP&ndash:50 and AP&ndash:DW. Fractions were examined for their molecular structure and their effects on sheep ruminal enzymes and solubilization of rubisco in vitro. All fractions significantly (p &lt: 0.05) inhibited the activity of ruminal glutamic oxaloacetic transaminase and glutamic pyruvic transaminase. The fractions AP&ndash:50 and EJ&ndash:50 significantly inhibited the activity of the R-cellulase enzyme. Most of the fractions inhibited R-glutamate dehydrogenase activity (p &lt: 0.05) by increasing its concentration, while protease activity decreased by up to 58% with increasing incubation time and concentration. The solubilization of rubisco was observed to be comparatively higher in A. pendula (16.60 &plusmn: 1.97%) and E. jambolana (15.03 &plusmn: 1.06%) than that of wheat straw (8.95 &plusmn: 0.95%) and berseem hay (3.04 &plusmn: 0.08%). A significant (p &lt: 0.05) increase in protein solubilization was observed when wheat straw and berseem hay were supplemented with A. pendula and E. jambolana leaves at different proportions. The efficiency of microbial protein was significantly (p &lt: 0.05) greater with the supplementation of leaves of A. pendula in comparison to E. jambolana. The overall conclusion is that the proanthocyanidins obtained from E. jambolana exhibited greater inhibitory activities on rumen enzymes, whereas A. pendula recorded higher protein solubilization. Thus, PAs from A. pendula and E. jambolana appear to have the potential to manipulate rumen enzyme activities for efficient utilization of protein and fiber in ruminants.