Isolation and Properties of Major Components of Penicillium canescens Extracellular Enzyme Complex

Синицына, О. А.; Bukhtoyarov, F. E.; Gusakov, Alexander V.; Окунев, О. Н.; Bekkarevitch, A. O.; Vinetsky, Yu. P.; Sinitsyn, A. P.

doi:10.1023/b:biry.0000009134.48246.7e

Cited by 56 publications

(26 citation statements)

References 11 publications

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“…A modification of the initial pH to 5, 6, 7.5, or 8 (by adjusting with a solution of NaOH 1% or HCl 37%) reduced the xylanase production to 6,440±278, 7,427±376, 6,786±279, and 7,640±521 U/g, respectively. Xylanase of P. canescens exhibits a pH-dependent behavior with an optimal stability at neutral pH [24]. In general, all the xylanases from the genus Penicillium are tightly regulated by the pH, expressing their transcripts at neutral pH only [20].…”

Section: Influence Of Additives On Xylanase Productionmentioning

confidence: 99%

Xylanase Production by Penicillium canescens on Soya Oil Cake in Solid-State Fermentation

Antoine

Destain

Thonart

2009

Appl Biochem Biotechnol

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There is an increasing interest for the organic residues from various sectors of agriculture and industries over the past few decades. Their application in the field of fermentation technology has resulted in the production of bulk chemicals and value-added products such as amino acid, enzymes, mushroom, organic acids, single-cell protein, biologically active secondary metabolites, etc. (Ramachandran et al., Bioresource Technology 98:2000-2009, 2007). In this work, the production of extracellular xylanase by the fungus Penicillium canescens was investigated in solid-state fermentation using five agro-industrial substrates (soya oil cake, soya meal, wheat bran, whole wheat bran, and pulp beet). The best substrate was the soya oil cake. In order to optimize the production, the most effective cultivation conditions were investigated in Erlenmeyer flasks and in plastic bags with 5 and 100 g of soya oil cake, respectively. The initial moisture content, initial pH, and temperature of the culture affected the xylanase synthesis. The optimal fermentation medium was composed by soya oil cake crushed to 5 mm supplemented with 3% and 4% (w/w) of casein peptone and Na(2)HPO(4) x 2H(2)O. After 7 days of incubation at 30 degrees C and under 80% of initial moisture, a xylanase production level of 18,895 +/- 778 U/g (Erlenmeyer flasks) and 9,300 +/- 589 U/g (plastic bags) was reached. The partially purified enzyme recovered by ammonium sulfate fractionation was completely stable at freezing and refrigeration temperatures up to 6 months and reasonably stable at room temperature for more than 3 months.

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Section: Influence Of Additives On Xylanase Productionmentioning

confidence: 99%

Xylanase Production by Penicillium canescens on Soya Oil Cake in Solid-State Fermentation

Antoine

Destain

Thonart

2009

Appl Biochem Biotechnol

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“…28) However, -L-arabinofuranosidases from Penicillium capsulatum 29) and P. purpurogenum 30) have displayed optimum activity at pH 4.0, whereas that from Penicillium canescens 31) has shown an optimal pH in the range of 5.0 to 6.5. As far as the authors are aware, no -L-arabinofuranosidase activity from P. funiculosum has been characterized with regards to its optimum pH.…”

Section: )mentioning

confidence: 99%

“…However, their optimal temperatures fell within the range of 50 to 70 C, as reported for hemicellulases from other fungi. [19][20][21]29,31,34) For instance, endo-1,4--D-xylanase and -D-xylosidase from P. funiculosum have been reported to display optimum activity at 55 and 60 C, respectively.…”

Section: )mentioning

confidence: 99%

“…4) also indicate that the specific activities of both endo-1,4--D-xylanase and endo-1,3-1,4--D-glucanase were less thermostable than those of -D-xylosidase and -L-arabinofuranosidase at temperatures above 60 C. Similarly, -D-xylosidase from Aspergillus awamori has shown higher thermal stability at 70 C than endo-1,4--D-xylanases from the same strain which rapidly lost their activity above 55 C. 12) As a whole, the hemicellulolytic activities present in the multi-enzymatic system from P. funiculosum showed thermal stability quite similar to that of the majority of fungal hemicellulases described in the literature. 17,19,20,29,31,34) Kinetic parameters In spite of the complexity of the multi-enzymatic system produced by P. funiculosum, it was still considered important to determine the apparent kinetic parameters of the selected hemicellulolytic enzymes. The apparent Michaelis-Menten constants, K mapp and V maxapp , estimated by non-linear regression are given in Table 1.…”

Section: )mentioning

confidence: 99%

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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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“…These poorly understood regioselectivities may explain at least in part the production of multiple ABFs by some fungi. Both Aspergillus terreus (24,25) and Penicillium purpurogenum (10) secrete three ABFs, and two are produced by Aspergillus awamori (22), Aspergillus niger (27), Penicillium capsulatum (12), Penicillium canescens (34), and Penicillium chrysogenum (29).…”

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Novel Bifunctional α-l-Arabinofuranosidase/Xylobiohydrolase (ABF3) fromPenicillium purpurogenum

Ravanal

Callegari

Eyzaguirre

2010

Appl Environ Microbiol

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The soft rot fungus Penicillium purpurogenum grows on a variety of natural substrates and secretes various isoforms of xylanolytic enzymes, including three arabinofuranosidases. This work describes the biochemical properties as well as the nucleotide and amino acid sequences of arabinofuranosidase 3 (ABF3). This enzyme has been purified to homogeneity. It is a glycosylated monomer with a molecular weight of 50,700 and can bind cellulose. The enzyme is active with p-nitrophenyl ␣-L-arabinofuranoside and p-nitrophenyl ␤-D-xylopyranoside with a K m of 0.65 mM and 12 mM, respectively. The enzyme is active on xylooligosaccharides, yielding products of shorter length, including xylose. However, it does not hydrolyze arabinooligosaccharides. When assayed with polymeric substrates, little arabinose is liberated from arabinan and debranched arabinan; however, it hydrolyzes arabinose and releases xylooligosaccharides from arabinoxylan. Sequencing both ABF3 cDNA and genomic DNA reveals that this gene does not contain introns and that the open reading frame is 1,380 nucleotides in length. The deduced mature protein is composed of 433 amino acids residues and has a calculated molecular weight of 47,305. The deduced amino acid sequence has been validated by mass spectrometry analysis of peptides from purified ABF3. A total of 482 bp of the promoter were sequenced; putative binding sites for transcription factors such as CreA (four), XlnR (one), and AreA (three) and two CCAAT boxes were found. The enzyme has two domains, one similar to proteins of glycosyl hydrolase family 43 at the amino-terminal end and a family 6 carbohydrate binding module at the carboxyl end. ABF3 is the first described modular family 43 enzyme from a fungal source, having both ␣-L-arabinofuranosidase and xylobiohydrolase functionalities.The simple sugar L-arabinose is the most common pentose with the L-configuration present in nature. It is found principally in plant cell wall components such as pectin and xylan. In pectin it is present in the arabinan backbone and side chains and in the arabinogalactan side chains. In xylan it is found as side chains of arabinoxylan (3).The biodegradation of plant cell wall polysaccharides is an important biotechnological process for obtaining monosaccharides useful in different industrial applications, such as fermentation for the generation of bioethanol (28). Among the enzymes participating in this process are those releasing arabinose residues. These include endo-acting arabinanases (hydrolyzing arabinan backbone) and exo-acting arabinofuranosidases (ABFs), which hydrolyze arabinofuranose side chains (3). Considering the variety of substrates and linkages associated with arabinofuranose-derived complex polysaccharides, the existence of a number of ABFs with different specificities can be envisioned.␣-L-Arabinofuranosidases (␣-L-arabinofuranoside arabinofuranohydrolases; EC 3.2.1.55) are exo-acting enzymes which hydrolyze nonreducing arabinofuranose residues from arabinoxylan, pectins, and shorter oligosaccharides. T...

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Isolation and Properties of Major Components of Penicillium canescens Extracellular Enzyme Complex

Cited by 56 publications

References 11 publications

Xylanase Production by Penicillium canescens on Soya Oil Cake in Solid-State Fermentation

Xylanase Production by Penicillium canescens on Soya Oil Cake in Solid-State Fermentation

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

Novel Bifunctional α-l-Arabinofuranosidase/Xylobiohydrolase (ABF3) fromPenicillium purpurogenum

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