Cloning of an acidic laccase gene (clac2) from Coprinus congregatus and its expression by external pH

Kim, S

doi:10.1016/s0378-1097(01)00003-9

Cited by 4 publications

(5 citation statements)

References 18 publications

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“…The pH 5.0~6.0 in the culture supernatant grown at 100 rpm was lower than pH 7.1~7.5 grown at 150 rpm. Many fungal laccases were induced and showed the higher activity at acidic conditions (Kim et al, 2001), and this result also followed the similar pattern. The higher mycelial concentration in the inoculum seemed to increase the laccase activity faster than the lower mycelial concentration at both 100 and 150 rpm of shaking conditions, but the differences were not significant (data not shown).…”

supporting

confidence: 70%

Effect of fungal pellet morphology on enzyme activities involved in phthalate degradation

Kim

Song

2009

J Microbiol.

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Pellet size of white rot fungus, Pleurotus ostreatus may affect the secretion of its degradative enzymes and accompanying biodegrading capability, but could be controlled by several physical culture conditions in liquid culture. The pellet size of P. ostreatus was affected by the volume of inoculum, flask, and medium, but the agitation speed was the most important control factor. At the lower agitation speed of 100 rpm, the large pellets were formed and the laccase activity was higher than that of small pelleted culture at 150 rpm, which might be due to loose intrapellet structure. However, the biodegradation rates of benzylbutylphthalate and dimethylphthalate were higher in the small pelleted culture, which indicated the involvement of other degradative enzyme rather than laccase. The activity of esterase which catalyzes the nonphenolic compounds before the reaction of ligninolytic enzymes was higher in the small pelleted culture, and coincided with the degradation pattern of phthalates. This study suggests the optimization of pellet morphology and subsequent secretion of degradative enzymes is necessary for the efficient removal of recalcitrants by white rot fungi.

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supporting

confidence: 70%

Effect of fungal pellet morphology on enzyme activities involved in phthalate degradation

Kim

Song

2009

J Microbiol.

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“…Chromosomal DNA from CL1407b was isolated [2] and digested with the Eco RV restriction enzyme, which has no recognition site in plasmid pBARGEM7‐1. The digested DNA fragments were separated on a 1% agarose gel, and DNAs longer than 4.5 kb were eluted from the gel.…”

Section: Methodsmentioning

confidence: 99%

“…Coprinellus congregatus is a mushroom‐forming basidiomycete, and its development is very easily manipulated in lab conditions [1]. There are two or more laccase isozymes implicated in the mushroom development, and the cDNA of the acidic laccase gene ( clac2 ) has been cloned [2]. Genetic transformation to phosphinothricin resistance has been carried out by restriction enzyme‐mediated integration (REMI) in C. congregatus , and several mutants that showed different growing patterns have been reported [3].…”

Section: Introductionmentioning

confidence: 99%

Tagging and localization of a phospholipase D gene inCoprinellus congregatusby restriction enzyme-mediated integration and pulsed-field gel electrophoresis

Leem

Ross

Choi

2003

FEMS Microbiology Letters

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We have identified a phospholipase D gene (pld) fragment from a transformant generated by restriction enzyme-mediated integration in Coprinellus congregatus, which is a mushroom-forming basidiomycete. A fragment of pld of this fungus has been cloned from a transformant by gene tagging. The transformation vector has been inserted into pld and this has resulted in a decreased enzyme activity of the transformant compared with the wild strain. C. congregatus has seven chromosomes, the range of its genome size is 1.6^4.7 Mb and pld is located at chromosome 4 where the transformation vector has been inserted.

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“…이 효소의 cDNA (lac2)를 확보하고 northern blot 분석 을 통하여 중성에서는 발현되지 않고 산성 조건에서만 발현됨 을 확인하였다 (Kim et al, 2001). 이 유전자의 발현 양상을 분 석하고자 promoter 및 genomic DNA 유전자를 cloning하였다 (Kim et al, 2006).…”

Section: Congregatus를 중성 액체배지에서 배양하면 상등액에는unclassified

Analysis of an acid-responsive element in a promoter of laccase gene in the inky cap, Coprinellus congregatus

Kim¹,

Nguyen²,

Choi³

2016

The Korean Journal of Microbiology

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ABSTRACT:The inky cap, Coprinellus congregatus, produces several laccase isozymes during its life cycle: both hyphal tip laccase and sclerotial laccase are involved in the fungal development. When this fungus was transferred to an acid liquid medium (pH 4.0-4.5), a new laccase was synthesized and secreted into the culture supernatant. In order to examine its regulation by external pH, green fluorescent protein gene was ligated at the downstream of the promoters having different lengths. These expression vectors having different promoter lengths were inserted into the fungal transformation vector, pBARGEM7-1. These expression vectors were introduced to the mating type a1 and a2 monokaryons, and the transformants were selected by the phosphinothricin resistance. Transformant a1 (a1TF) and transformant a2 (a2TF) were mated with each other to generate homozygotic dikaryon transformants. All these transformants were grown in neutral liquid medium for 5 days, and then the whole cell homogenates were transferred to the acidic liquid medium (pH 4.1). After 36 h incubation at 25°C, cells were harvested for the analysis of GFP expression. GFP expression was detected in the transformant having full-length promoter (2.0 kb), but other transformants having shorter length promoter (shorter than 1.29 kb) failed to show the fluorescence. Therefore, the acid-responsive element in the laccase promoter should be localized between -2.0 kb ~ -1.29 kb region.

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Cloning of an acidic laccase gene (clac2) from Coprinus congregatus and its expression by external pH

Cited by 4 publications

References 18 publications

Effect of fungal pellet morphology on enzyme activities involved in phthalate degradation

Effect of fungal pellet morphology on enzyme activities involved in phthalate degradation

Tagging and localization of a phospholipase D gene inCoprinellus congregatusby restriction enzyme-mediated integration and pulsed-field gel electrophoresis

Analysis of an acid-responsive element in a promoter of laccase gene in the inky cap, Coprinellus congregatus

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