The role of N-glycosylation on the enzymatic activity of a Pycnoporus sanguineus laccase

Vite-Vallejo, Odón; Palomares, Laura A.; Dantán-González, Edgar; Ayala-Castro, Hector G.; Martínez‐Anaya, Claudia; Valderrama, Brenda; Folch-Mallol, Jorge Luis

doi:10.1016/j.enzmictec.2009.05.007

Cited by 60 publications

(44 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The cultivation time necessary to reach the highest laccase activities was considerably reduced from 28 to 13 d, with a total productivity increment of 26 times. To the best of our knowledge, the levels of laccase activity achieved by P. sanguineus CS43 in stirred tank bioreactor runs (143 000 IU/L) are the highest reported in the literature (Lomascolo et al, 2002;van der Merwe, 2002;Litthauer et al, 2007;Vanhulle et al, 2007a;Dantán-González et al, 2008;Vite-Vallejo et al, 2009;Uzan et al, 2010). Uzan et al (2010) previously reported high laccase production (83 700 IU/L) in flasks using a Chinese strain of P. sanguineus induced by ethanol (30 g/L) which is similar to the activity obtained at shaken flask level in the present study.…”

Section: Discussionmentioning

confidence: 85%

Enhanced production of thermostable laccases from a native strain of Pycnoporus sanguineus using central composite design

Ramírez-Cavazos

Junghanns

Nair

et al. 2014

J. Zhejiang Univ. Sci. B

View full text Add to dashboard Cite

Abstract:The production of thermostable laccases from a native strain of the white-rot fungus Pycnoporus sanguineus isolated in Mexico was enhanced by testing different media and a combination of inducers including copper sulfate (CuSO 4 ). The best conditions obtained from screening experiments in shaken flasks using tomato juice, CuSO 4 , and soybean oil were integrated in an experimental design. Enhanced levels of tomato juice as the medium, CuSO 4 and soybean oil as inducers (36.8% (v/v), 3 mmol/L, and 1% (v/v), respectively) were determined for 10 L stirred tank bioreactor runs. This combination resulted in laccase titer of 143 000 IU/L (2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid), pH 3.0), which represents the highest activity so far reported for P. sanguineus in a 10-L fermentor. Other interesting media resulting from the screening included glucose-bactopeptone which increased laccase activity up to 20 000 IU/L, whereas the inducers Acid Blue 62 and Reactive Blue 19 enhanced enzyme production in this medium 10 times. Based on a partial characterization, the laccases of this strain are especially promising in terms of thermostability (half-life of 6.1 h at 60 °C) and activity titers.

show abstract

Section: Discussionmentioning

confidence: 85%

Enhanced production of thermostable laccases from a native strain of Pycnoporus sanguineus using central composite design

Ramírez-Cavazos

Junghanns

Nair

et al. 2014

J. Zhejiang Univ. Sci. B

View full text Add to dashboard Cite

show abstract

“…The purification and characterization of laccases from the leading producers of white-rot fungi had been greatly reported [9][10][11][12]. For commercial applications, it usually requires unique properties such as the thermal stability and resistant to acid or alkaline under some harsh conditions.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of two thermostable laccases with high cold adapted characteristics from Pycnoporus sp. SYBC-L1

Wang

Cai

Liao

et al. 2010

Process Biochemistry

View full text Add to dashboard Cite

“…The average glycosylation of laccases is usually between 10 and 25% (Baldrian, 2006). Glycosylation influences enzyme secretion, and it has been suggested to play an important role in catalytic center stabilization, protection against hydrolysis, copper retention, and laccase thermal stability (Vite-Vallejo et al, 2009). Taken together, these results suggest that it would be important to experimentally evaluate the functions of the laccase gene families identified among these plant pathogens.…”

Section: Discussionmentioning

confidence: 99%

Exploring laccase genes from plant pathogen genomes: a bioinformatic approach

Feng

et al. 2015

Genet. Mol. Res.

View full text Add to dashboard Cite

ABSTRACT. To date, research on laccases has mostly been focused on plant and fungal laccases and their current use in biotechnological applications. In contrast, little is known about laccases from plant pathogens, although recent rapid progress in whole genome sequencing of an increasing number of organisms has facilitated their identification and ascertainment of their origins. In this study, a comparative analysis was performed to elucidate the distribution of laccases among bacteria, fungi, and oomycetes, and, through comparison of their amino acids, to determine the relationships between them. We retrieved the laccase genes for the 20 publicly available plant pathogen genomes. From these, 125 laccase genes were identified in total, including seven in bacterial genomes, 101 in fungal genomes, and 17 in oomycete genomes. Most of the predicted protein models of these genes shared typical fungal laccase characteristics, possessing four conserved domains with one cysteine and ten histidine residues at these domains. Phylogenetic analysis illustrated that laccases from bacteria and oomycetes were grouped into two distinct clades, whereas fungal laccases clustered in three main clades. These results 14019-14036 (2015) provide the theoretical groundwork regarding the role of laccases in plant pathogens and might be used to guide future research into these enzymes.

show abstract

The role of N-glycosylation on the enzymatic activity of a Pycnoporus sanguineus laccase

Cited by 60 publications

References 34 publications

Enhanced production of thermostable laccases from a native strain of Pycnoporus sanguineus using central composite design

Enhanced production of thermostable laccases from a native strain of Pycnoporus sanguineus using central composite design

Purification and characterization of two thermostable laccases with high cold adapted characteristics from Pycnoporus sp. SYBC-L1

Exploring laccase genes from plant pathogen genomes: a bioinformatic approach

Contact Info

Product

Resources

About