1996
DOI: 10.1021/bk-1996-0655.ch014
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MnP Isoenzymes Produced by Two Pleurotus Species in Liquid Culture and During Wheat-Straw Solid-State Fermentation

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Cited by 33 publications
(22 citation statements)
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“…3.35, the two B. adusta MnP are more acidic than most MnP isoenzymes (showing isoelectric points between 2.9 and 5.3). With respect to these unusual catalytic properties B. adusta MnP is similar to recently described MnP from Pleurotus species [13,23]. In contrast to the wellstudied MnP isoenzymes from P. chrysosporium [9], the B. adusta MnP1 and MnP2 exhibit manganeseindependent activity on aromatic substrates, such as veratryl alcohol and DMP.…”
Section: Atcpdgt-qlmnaeccallavrddlsupporting
confidence: 61%
See 1 more Smart Citation
“…3.35, the two B. adusta MnP are more acidic than most MnP isoenzymes (showing isoelectric points between 2.9 and 5.3). With respect to these unusual catalytic properties B. adusta MnP is similar to recently described MnP from Pleurotus species [13,23]. In contrast to the wellstudied MnP isoenzymes from P. chrysosporium [9], the B. adusta MnP1 and MnP2 exhibit manganeseindependent activity on aromatic substrates, such as veratryl alcohol and DMP.…”
Section: Atcpdgt-qlmnaeccallavrddlsupporting
confidence: 61%
“…After its description in P. chrysosporium [7] MnP isoenzymes were characterized from several white-rot fungi including Trametes versicolor [14,21,22] and Pleurotus species [13,23]. After its description in P. chrysosporium [7] MnP isoenzymes were characterized from several white-rot fungi including Trametes versicolor [14,21,22] and Pleurotus species [13,23].…”
Section: Discussionmentioning
confidence: 99%
“…This is also the case for S. commune SC3, whose expression is detected in both dikaryons and monokaryons (47). Finally, it should be kept in mind that this pattern of hydrophobin expression in submerged cultures can differ from solid fermentation processess as metabolism under these two culture conditions also differs (29,32,48).…”
Section: Discussionmentioning
confidence: 80%
“…The second group of peroxidases, VPs, is capable of oxidizing Mn 2+ via a mechanism similar to that described for MnPs (Ruiz-Dueñas et al 2007). Due to the VPs Mn 2+ -oxidizing activity, these enzymes were first described as MnP isoenzymes (Giardina et al 2000;Martínez et al 1996b) but later recognized as representing a new peroxidase type. VPs have a third active site on the enzyme surface, the exposed tryptophanyl radical (Trp-164), as found in LiP (Pérez-Boada et al 2005 (Doyle et al 1998;Blodig et al 2001;Smith et al 2009).…”
Section: Structure-function Relationshipmentioning
confidence: 99%