Novel peroxidases of Marasmius scorodonius degrade beta-carotene.

Two extracellular enzymes (MsP1 and MsP2) capable of efficient beta-carotene degradation were purified from culture supernatants of the basidiomycete Marasmius scorodonius (garlic mushroom). Under native conditions, the enzymes exhibited molecular masses of approximately 150 and approximately 120 kDa, respectively. SDS-PAGE and mass spectrometric data suggested a composition of two identical subunits for both enzymes.

A peroxidase from Lepista irina cleaves beta,beta-carotene to flavor compounds.

Extracellular liquid of the edible fungus Lepista irina was found to effectively degrade beta,beta-carotene, beta-lonone, beta-cyclocitral, dihydroactinidiolide, and 2-hydroxy-2,6,6-trimethylcyclohexanone were formed as volatile breakdown products of beta,beta-carotene with mycelium-free culture supernatants, whereas beta-apo-10'-carotenal was identified as non-volatile degradation product. The key enzyme catalyzing the oxidative cleavage of beta,beta-carotene was purified with an overall yield of 63% and a purification factor of 43. Biochemical characterization showed a molecular mass of 50.