1980
DOI: 10.1099/00221287-117-2-327
|View full text |Cite
|
Sign up to set email alerts
|

Production, Purification and Properties of Extracellular Laccase of Agaricus bisporus

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

14
103
1
1

Year Published

1984
1984
2008
2008

Publication Types

Select...
9
1

Relationship

1
9

Authors

Journals

citations
Cited by 127 publications
(122 citation statements)
references
References 32 publications
14
103
1
1
Order By: Relevance
“…These data are consistent with other studies showing optima pH values for other fungal species, like Pycnoporus cinnabarinus (pH 4.0) (7), Lentinula edodes (pH 4.0) (5) and Coprinus cinereus (4.0) (25). The two activity peaks detected suggest the presence of an isozyme or indicate that this laccase presents two distinct pH optima, like observed in Agaricus bisporus (32) and Monocillium saxena (28). No laccase activity was detected at pH values higher than 6.5, which is in agreement with findings for other fungal species, such as L. edodes (5,33).…”
supporting
confidence: 81%
“…These data are consistent with other studies showing optima pH values for other fungal species, like Pycnoporus cinnabarinus (pH 4.0) (7), Lentinula edodes (pH 4.0) (5) and Coprinus cinereus (4.0) (25). The two activity peaks detected suggest the presence of an isozyme or indicate that this laccase presents two distinct pH optima, like observed in Agaricus bisporus (32) and Monocillium saxena (28). No laccase activity was detected at pH values higher than 6.5, which is in agreement with findings for other fungal species, such as L. edodes (5,33).…”
supporting
confidence: 81%
“…The size of the nascent polypeptide obtained by in vitro translation and immunoprecipitation was estimated to be 57 kDa (Perry et al, 1993) which is in accord with the above calculated mass values. The calculated isoelectric pH of the products of lccl and lcc2 differ by a readily detectable amount, but as extracellular laccase focuses as a diffuse band at pH 3.4-4.0 (Wood, 1980a), the glycosylated enzyme is significantly more negatively charged than calculated for either of the non-glycosylated polypeptide(s). Both lccl and lcc2 products have five potential N-glycosylation sites (Fig.…”
Section: The Deduced Amino Acid Sequence Of Lccl and Lcc2mentioning
confidence: 99%
“…The ability of fungal laccases to oxidize lignin-related phenolic compounds suggests that these enzymes play a role in lignin degradation (Eriksson e t al., 1990). Laccases have been isolated from various fungi and their physiological functions have been discussed (Froehner & Eriksson, 1974;Wood, 1980;De Vries et al, 1986 Rehman & Thurston, 1992;Jeong e t al., 1992). The white-rot fungus Plezlrotzls ostreatzls is a well-known lignin-degrader (Agosin e t al., 1985) and it can produce various enzymes, such as extracellular peroxidase (Kang et al, 1993), veratryl alcohol oxidase (Sannia e t al., 1991), glucose oxidase (Shin e t al., 1993) and laccase (Sannia e t al., 1986;Kim e t al., 1987), all of which are related to lignin degradation.…”
Section: Single Electron Transfer By An Extracellular Laccase From Thmentioning
confidence: 99%