Exploring glutathione lyases as biocatalysts: paving the way for enzymatic lignin depolymerization and future stereoselective applications. Issue 11 (28th July 2015)

• Record Type: Journal Article
• Authors: Picart, Pere; Sevenich, Marc; Domínguez de María, Pablo; Schallmey, Anett
• Is Part Of: Green chemistry. Volume 17:Issue 11(2015)
• Page Start: 4931
• Page End: 4940
• Publication Date: 2015-07-28
• Subjects: Environmental chemistry -- Industrial applications -- Periodicals; Environmental management -- Periodicals; 660
• DOI: 10.1039/c5gc01078k
• Languages: English
• ISSNs: 1463-9262

Abstract

Abstract : One pot – two enzymes . The combination of β-etherases with glutathione lyases enables the selective cleavage of lignin model compounds. Protein engineering of glutathione lyases allows modification of activity and stereoselectivity. Abstract : Glutathione-dependent β-etherases and glutathione lyases are key-enzymes for the biocatalytic depolymerization of lignin. In the first step, the nucleophilic attack of glutathione to the common β- O -4-aryl-ether motif in lignin is catalyzed by β-etherases and afterwards the glutathione is removed again by the action of glutathione lyases. Given their potential impact for lignin valorization, in this paper novel glutathione lyases are reported and biocatalytically characterized based on lignin model compounds. As a result, an enzyme exhibiting increased thermostability and lowered enantioselectivity – key features for implementation of glutathione lyases in enzymatic lignin depolymerization processes – was identified. Furthermore, first mutational studies of these enzymes revealed the possibility to further alter the activity as well as enantioselectivity of glutathione lyases by means of protein engineering. From a practical perspective, one-pot multi-step processes combining β-etherases and glutathione lyases are successfully set-up, giving hints on the potential that the implementation of these biocatalysts may bring for biorefinery purposes.