LIGNINASE FROM PHANEROCHAETE CHRYSOSPORIUM: CATALYTIC PROPERTIES OF A NOVEL ENZYME.

T. Kent Kirk, Ming Tien, Kenneth E. Hammel, Philip Kersten, B. Kalyanaraman

Research output: Chapter in Book/Report/Conference proceedingConference contribution

1 Scopus citations

Abstract

Ligninase isolated from Phanerochaete chrysosporium catalyzes cleavage of beta -1 and beta -0-4 lignin models between C// alpha and C// beta of their propyl side chains, and it also catalyzes a number of other oxidations in various lignin-related compounds. Some of the reactions, including C// alpha -C// beta cleavage, consume both H//2O//2 and O//2, whereas others consume only H//2O//2. Based on studies of the mechanism of oxidation of several substrates, a unified scheme for ligninase action on lignin-related compounds is proposed.

Original languageEnglish (US)
Title of host publicationUnknown Host Publication Title
Pages243-248
Number of pages6
StatePublished - Dec 1 1985

All Science Journal Classification (ASJC) codes

  • Engineering(all)

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