Enzymatische Versuche zur Entstehung des Lignins.

Freudenberg, Karl; Richtzenhain, Hermann

doi:10.1515/hfsg.1947.1.3.90

Cited by 8 publications

(6 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since the 1950s, various oxidases have been implicated as having roles in lignification -these have included peroxidase (12,53,54,171,(254)(255)(256)(257), laccase (12,53,54,(258)(259)(260)(261)(262)(263)(264)(265)(266), combined peroxidase and laccase (12,53,54,254,267), coniferyl alcohol oxidase (268)(269)(270)(271), (poly)phenol oxidase (272)(273)(274)(275)(276)(277)(278), and cytochrome oxidase (279). Their putative involvement has generally relied upon the ability of such enzymes to oxidize monolignols in vitro, even though none of these enzymes have yet engendered formation of products in vitro that duplicate faithful facsimiles of lignin structure; in some cases, they do not even generate formation of polymeric products.…”

Section: The Enigma Of Monolignol Radical Generationmentioning

confidence: 99%

“…The early suggestions that a polyphenol oxidase might be involved emerged from studies by Freudenberg in 1953, using a press-sap extract of the mushroom, Agaricus campestris (272)(273)(274)(275)(276)(277) and also later by Mason and Cronyn (278); mushrooms do not, however, biosynthesize lignins. Another candidate was coniferyl alcohol oxidase, detected in jack pine (Pinus strobus) (268,269), other Pinaceae species (268,269,271) and tobacco (270); this has also not been demonstrated to either afford lignins in vitro and/or have a role in lignification in vivo.…”

Section: Proteins With No Yet Established Roles In Lignificationmentioning

confidence: 99%

See 1 more Smart Citation

Lignins: A Twenty‐First Century Challenge

Davin

Patten

Jourdes

et al. 2008

Biomass Recalcitrance

View full text Add to dashboard Cite

Section: The Enigma Of Monolignol Radical Generationmentioning

confidence: 99%

Section: Proteins With No Yet Established Roles In Lignificationmentioning

confidence: 99%

Lignins: A Twenty‐First Century Challenge

Davin

Patten

Jourdes

et al. 2008

Biomass Recalcitrance

View full text Add to dashboard Cite

“…In an interesting series of papers Freudenberg and Richtzenhain (31,32), and later Richtzenhain (77, 78, 79) reported researches on the enzyme-catalyzed polymerization of lignin-related compounds. The enzyme was obtained by extracting the sporophores of Agaricus campestris with water and subsequent fractionation of the water extract with alcohol to give a dry powder.…”

Section: Miscellaneous Studiesmentioning

confidence: 99%

Microbiological Aspects of Lignin Degradation 1

Gottlieb¹,

Pelczar²

1951

Bacteriological Reviews

View full text Add to dashboard Cite

With the current increased emphasis on the utilization of by-products from large industrial operations, the potential utilization by-product lignin is attracting considerable attention. In 1944, 188,500,000 tons of wood were cut in the 1 This review was prepared in connection with investigations in progress under contract No. N7 onr 397-4 between the University of Maryland and the Office of Naval Research.

show abstract

“…Five decades ago, Freudenberg and Richtzenhain (1943) produced a lignin-like material, dehydrogenation polymer (DHP), by dehydrogenative polymerization of coniferyl alcohol with press-sap of champignon in the presence of oxygen. Eventually, the major enzyme in the press-sap of champignon was identified to be laccase (Benzendiol: Oxygen Oxidoreductase; EC 1.10.3.1).…”

Section: Introductionmentioning

confidence: 99%

Comparative Studies on Dehydrogenative Polymerization of Coniferyl Alcohol by Laccases and Peroxidases. Part 1. Preliminary Results

Okusa¹,

Miyakoshi²,

Chen³

1996

HFSG

View full text Add to dashboard Cite

Laccase from Rhus vernicifera Stokes oxidized coniferyl alcohol (1) very slowly in acetone-Water (1:1, v/v) in the presence of molecular oxygen. At the reaction time of 144hrs, about 20mol% of pinoresinol (2), 25mol% of dehydrodiconiferyl alcohol (3), and 2mol% of guaiacylglycerol-ß-coniferyl ether (4) were produced, but no dehydrogenative polymer (DHP). Laccases from Coriolus versicolor and Pycnoporus coccineus oxidized the substrate faster than Rhus laccase. At the reaction time of 1.5 hrs, Coriolus iaccase oxidized the substrate, producing all three dimers and a trace amount of DHP, and Pycnoporus laccase producing dimers 2 and 3 but no DHP. At the reaction time of 12hrs, Coriolus laccase oxidized the substrate, producing all three dimers and a small amount of DHP, and Pycnoporus laccase producing only DHP but no dimers. Peroxidase type I and II from horseradish (Armoracia rusticana) oxidized the substrate even faster than the laccases in acetone-water (1:4, v/v) in the presence of hydrogen peroxide, producing DHP predominately at the reaction time of 5 hrs. Tree-laccases may differ from fungal laccases in the oxidation rate and reaction mechanisms. This is probably due to differences in the nature and molecular mass of these glycoproteins, as well as the ligand binding mode of type 2 and type 3 copper sites. During the oxidation by the laccases and peroxidases, the substrate and polymeric products could also undergo biodegradation. The possible role of laccase in biosynthesis of lignin is discussed.

show abstract

Enzymatische Versuche zur Entstehung des Lignins.

Cited by 8 publications

References 0 publications

Lignins: A Twenty‐First Century Challenge

Lignins: A Twenty‐First Century Challenge

Microbiological Aspects of Lignin Degradation 1

Comparative Studies on Dehydrogenative Polymerization of Coniferyl Alcohol by Laccases and Peroxidases. Part 1. Preliminary Results

Contact Info

Product

Resources

About