Sequencing of a 1,3-1,4-beta-D-glucanase (lichenase) from the anaerobic fungus Orpinomyces strain PC-2: properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin

Chen, H; Li, X L; Ljungdahl, Lars G.

doi:10.1128/jb.179.19.6028-6034.1997

Cited by 93 publications

(112 citation statements)

References 52 publications

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“…12,25) Hemicellulases classified as endo-1,3-1,4--D-glucanase are mainly produced by plants and bacteria; as far as the authors are aware, only two endo-1,3-1,4--Dglucanases have been isolated from a fungal source, including anaerobic Orpinomyces sp. 26) and thermophilic aerobic Talaromyces emersonii.…”

Section: )mentioning

confidence: 99%

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

Karboune¹,

L’Hocine²,

Anthoni³

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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A multi-enzymatic system from Penicillium funiculosum displayed -L-arabinofuranosidase, endo-1,4--Dxylanase, -D-xylosidase and endo-1,3-1,4--D-glucanase activities at high levels over a wide acidic pH range of 2.0 to 5.5. Moreover, the pH stability was particularly extended over the wide range of pH of 2.0 to 8.0 with endo-1,3-1,4--D-glucanase and endo-1,4--D-xylanase; however, -L-arabinofuranosidase and -D-xylosidase exhibited higher stability in the pH range of 2.0 to 5.5. The results indicate that the optimal temperature of -L-arabinofuranosidase (65 C) and -D-xylosidase (70 C) as well as their thermal stability were higher than those of endo-1,3-1,4--D-glucanase (60 C) and endo-1,4--D-xylanase (50 C). Although V maxapp of -Dxylosidase and endo-1,4--D-xylanase was higher than that of -L-arabinofuranosidase and endo-1,3-1,4--Dglucanase, respectively, their catalytic efficiency was lower. High levels of ferulolyl esterase, -D-galactosidase, -D-mannosidase and endo-1,4--D-mannanase activities were also detected in the multi-enzymatic system. The overall features of the multi-enzymatic system from P. funiculosum reveal its potential for degrading and modifying plant cell walls from a variety of food and feedstuffs.

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Section: )mentioning

confidence: 99%

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

Karboune¹,

L’Hocine²,

Anthoni³

et al. 2009

Bioscience, Biotechnology, and Biochemistry

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“…Although anaerobic fungi are true eukaryotic microorganisms, previous reports suggested that some rumen fungal enzyme genes were originated from bacteria (Gilbert et al1992;Zhou et al 1994;Chen et al 1997). Therefore, xyn2A was successfully expressed in E. coli under the control of bacterial promoter lacZ.…”

Section: Discussionmentioning

confidence: 99%

Cloning of a xylanase gene xyn2A from rumen fungus Neocallimastix sp. GMLF2 in Escherichia coli and its partial characterization

et al. 2009

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Anaerobic fungi belonging to the family Neocallimastigaceae are native inhabitants in the rumen of the most herbivores, such as cattle, sheep and goats. A member of this unique group, Neocallimastix sp. GMLF2 was isolated from cattle feces and screened for its xylanase encoding gene using polymerase chain reaction. The gene coding for a xylanase (xyn2A) was cloned in Escherichia coli and expression was monitored. To determine the enzyme activity, assays were conducted for both fungal xylanase and cloned xylanase (Xyl2A) for supernatant and cell-associated activities. Optimum pH and temperature of the enzyme were found to be 6.5 and 50• C, respectively. The enzyme was stable at 40• C and 50• C for 20 min but lost most of its activity when temperature reached 60• C for 5-min incubation time. Rumen fungal xylanase was mainly released to the supernatant of culture, while cloned xylanase activity was found as cell-associated. Multiple alignment of the amino acid sequences of Xyl2A with published xylanases from various organisms suggested that Xyl2A belongs to glycoside hydrolase family 11.

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“…The deduced amino acid sequence of the enzyme was identical to those of LicA from Orpinomyces sp. Strain PC-2, 3) although there was a two-nucleotide dissimilarity between the glA and licA genes. We designed forward and reverse primers, glA-F (5?-CCGGGATCCATG-GCTCCTGCTCCCGCTCCTGTT-3?)…”

mentioning

confidence: 99%

“…Cross species sequence alignment had showed that most bacteria homologs of LicA, including highly thermostable Bacillus macerans b-glucanase, had valine in the position corresponding to LicA Asp-70. 3,6) Valine at this position may play a crucial role for the stability of this enzyme family. During With the hope of stepwise accumulation of beneˆ-cial mutations, 2011D was put through to DNA shuOEing, according to the method of Stemmer.…”

mentioning

confidence: 99%

A Variant ofOrpinomyces joyonii1,3-1,4-β-Glucanase with Increased Thermal Stability Obtained by Random Mutagenesis and Screening

Kim¹,

Cheng²,

Liu³

2002

Bioscience, Biotechnology, and Biochemistry

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Sequencing of a 1,3-1,4-beta-D-glucanase (lichenase) from the anaerobic fungus Orpinomyces strain PC-2: properties of the enzyme expressed in Escherichia coli and evidence that the gene has a bacterial origin

Cited by 93 publications

References 52 publications

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

Properties of Selected Hemicellulases of a Multi-Enzymatic System fromPenicillium funiculosum

Cloning of a xylanase gene xyn2A from rumen fungus Neocallimastix sp. GMLF2 in Escherichia coli and its partial characterization

A Variant ofOrpinomyces joyonii1,3-1,4-β-Glucanase with Increased Thermal Stability Obtained by Random Mutagenesis and Screening

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