EFFECT OF MONENSIN AND A PROTONOPHORE ON PROTEIN-DEGRADATION, PEPTIDE ACCUMULATION, AND DEAMINATION BY MIXED RUMINAL MICROORGANISMS INVITRO

Mixed ruminal bacteria (80 mg N/liter) degraded casein and soluble soy protein rapidly (.68 and .72 mg N/[liter.min], respectively), but ammonia was produced at a slower rate (.08 and .10 mg N/[liter.min], respectively). Because there was little increase in cell protein, ammonia production could not account for all the degraded protein. Large quantities of non-ammonia, non-protein nitrogen (NAN-NPN) accumulated, and this NAN-NPN reacted more strongly (2- to 14-fold) with ninhydrin after it was treated with 6 N HCl (110-degrees-C, 24 h) or pronase E. Even after 96 h of incubation, 10% of the protein N was still found in the NAN-NPN pool. Monensin had little effect on protein degradation, but it caused a large decrease in ammonia production (P < .05) and an increase in NAN-NPN (P < .05). These results indicated that significant quantities of peptide N could not be degraded by ruminal microorganisms and that monensin could increase peptide flow from the rumen. Because 3,3',4',5-tetrachlorosalicylanide, a protonophore that inhibits both Gram-positive and Gram-negative bacteria, did not cause a greater decrease (P > .05) in ammonia than monensin, an ionophore that is primarily effective against Gram-positive bacteria, it seemed that the "protein sparing" of monensin could largely be explained by its inhibition of Gram-positive bacteria.