Enzymatic hydrogenation of trans-2-nonenal in barley.
Conversion of undesirable, taste-active compounds is crucial for using barley as a suitable raw material for beer production. Here, ALH1, a barley alkenal hydrogenase enzyme that reduced the alpha,beta-unsaturated double bond of aldehydes and ketones, was found to convert trans-2-nonenal (T2N), a major contributor to the cardboard-like flavor of aged beer. Although the physiological function of ALH1 in barley development remains elusive, it exhibited high specificity with NADPH as a cofactor in the conversion of several oxylipins-including T2N, trans-2-hexenal, traumatin, and 1-octen-3-one. ALH1 action represents a previously unknown mechanism for T2N conversion in barley. Additional experimental results resolved the genomic sequence for barley ALH1, as well as the identification of a paralog gene encoding ALH2. Interestingly, T2N was not converted by purified, recombinant ALH2. The possibility to enhance ALH1 activity in planta is discussed--not only with respect to the physiological consequences thereof--but also in relation to improved beer quality.[1]References
- Enzymatic hydrogenation of trans-2-nonenal in barley. Hambraeus, G., Nyberg, N. J. Agric. Food Chem. (2005) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
