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Proteomics of secretomes from Agaricus bisporus grown on 12C-lignin

ABSTRACT: In the A. bisporus treated lignin (12CLg+Ab; pure lignin as sole C-source) secretome, a total of 500 (putative) proteins were detected, of which 72 were carbohydrate-active enzymes (CAZymes). Furthermore, we found 27 enzymes that are active on lignin and aromatics. Among those enzymes, 23 are classified as Auxiliary Activities (AA; CAZy.org), of which eight belong to subfamily AA1_1, another eight to subfamily AA3_2, five to subfamily AA5_1, and one to subfamilies AA1_2 and AA2. Interestingly, six AA1_1 members were annotated as sensu stricto laccases. Proteins from subfamilies AA5_1 and AA3_2 can be further categorized as glyoxal oxidases (GLOX) and aryl alcohol oxidases (AAO), respectively. These enzymes are likely involved in lignin modification and potentially supply peroxidases and peroxygenases with required H2O2. Among the CAZy-classified proteins, one manganese peroxidase (MnP) (AA2; ID 221245) was found, which likely is involved in ligninolysis. Two heme-containing unspecific peroxygenases (UPOs; ID 226793, 183842), were also secreted, and as previously suggested they may play a role in ligninolytic processes, either by demethylation, hydroxylation, or potentially by contributing to the cleavage of β-O-4′ ether linkages.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Agaricus Bisporus Var. Bisporus H97

TISSUE(S): Cell Suspension Culture, Fungal Cell

SUBMITTER: Mirjam Kabel

LAB HEAD: Mirjam A. Kabel

PROVIDER: PXD045077 | Pride | 2024-03-15

REPOSITORIES: Pride

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