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 Citation (Scopus)

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

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Lignin
Enzymes
Oxidation
Substrates

All Science Journal Classification (ASJC) codes

  • Engineering(all)

Cite this

Kent Kirk, T., Tien, M., Hammel, K. E., Kersten, P., & Kalyanaraman, B. (1985). LIGNINASE FROM PHANEROCHAETE CHRYSOSPORIUM: CATALYTIC PROPERTIES OF A NOVEL ENZYME. In Unknown Host Publication Title (pp. 243-248)
Kent Kirk, T. ; Tien, Ming ; Hammel, Kenneth E. ; Kersten, Philip ; Kalyanaraman, B. / LIGNINASE FROM PHANEROCHAETE CHRYSOSPORIUM : CATALYTIC PROPERTIES OF A NOVEL ENZYME. Unknown Host Publication Title. 1985. pp. 243-248
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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.",
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Kent Kirk, T, Tien, M, Hammel, KE, Kersten, P & Kalyanaraman, B 1985, LIGNINASE FROM PHANEROCHAETE CHRYSOSPORIUM: CATALYTIC PROPERTIES OF A NOVEL ENZYME. in Unknown Host Publication Title. pp. 243-248.

LIGNINASE FROM PHANEROCHAETE CHRYSOSPORIUM : CATALYTIC PROPERTIES OF A NOVEL ENZYME. / Kent Kirk, T.; Tien, Ming; Hammel, Kenneth E.; Kersten, Philip; Kalyanaraman, B.

Unknown Host Publication Title. 1985. p. 243-248.

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

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N2 - 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.

AB - 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.

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Kent Kirk T, Tien M, Hammel KE, Kersten P, Kalyanaraman B. LIGNINASE FROM PHANEROCHAETE CHRYSOSPORIUM: CATALYTIC PROPERTIES OF A NOVEL ENZYME. In Unknown Host Publication Title. 1985. p. 243-248