Beta-alanine suppresses heat inactivation of lactate dehydrogenase.

Beta-Alanine exhibits neurotransmitter activity and is a component of the anti-glycation agent carnosine. We propose that beta-alanine may have additional properties which may be of physiological significance. Interestingly, stress modulates the level of beta-alanine, which regulates excitotoxicity responses and prevents neuronal cell death. We hypothesize that beta-alanine's protective role may involve preservation of enzyme structure and function, suggesting that beta-alanine may act as a chemical chaperone. We used light scattering, enzyme activity and intrinsic fluorescence to monitor heat-induced changes in lactate dehydrogenase (LDH) in the presence and absence of beta-alanine. We observed that beta-alanine suppressed heat-induced LDH inactivation, prevented LDH aggregation, ameliorated the decrease in intrinsic fluorescence and reactivated thermally denatured LDH. These observations support the hypothesis that beta-alanine has chaperone-like activity and may play a cellular role in the preservation of enzyme function.