Purification and regulation of the synthesis of a β-xylosidase from Aspergillus nidulans

Kumar, S

doi:10.1016/0378-1097(95)00468-8

Cited by 32 publications

(48 citation statements)

References 5 publications

(6 reference statements)

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“…L. lactis IO-1 exhibited a significant level of intracellular xylosidase activity compared to other known xylosidase producers. Specific xylosidase activities of 1.2 U mg Ϫ1 , 0.21 U mg Ϫ1 , and 0.09 U mg Ϫ1 have been previously reported for Aspergillus nidulans (18), Bacillus sp. strain K-1 (25), and Clostridium cellulolyticum (29).…”

Section: Discussionmentioning

confidence: 61%

Genetic Evidence for a Defective Xylan Degradation Pathway in Lactococcus lactis

Erlandson

Delamarre

Batt

2001

Appl Environ Microbiol

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Section: Discussionmentioning

confidence: 61%

Genetic Evidence for a Defective Xylan Degradation Pathway in Lactococcus lactis

Erlandson

Delamarre

Batt

2001

Appl Environ Microbiol

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“…Several genes encoding xylanolytic enzymes have been studied with respect to regulation of expression, and all demonstrated expression in the presence of D-xylose, xylobiose, or xylan (78,93,108,126,222,292,382) but repression of expression in the presence of glucose (see "Carbon catabolite repression" below). Expression of some xylanolytic genes was also observed on L-arabinose (93,95,222). This might be due to the presence of small amounts of D-xylose in the L-arabinose preparations used, as detected in the L-arabinose preparation obtained from Sigma (R. P. de Vries, unpublished results).…”

Section: Regulation Of Gene Expression Coordinated Expression Of Genementioning

confidence: 99%

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

Vries

Visser

2001

Microbiol Mol Biol Rev

879

585

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SUMMARY Degradation of plant cell wall polysaccharides is of major importance in the food and feed, beverage, textile, and paper and pulp industries, as well as in several other industrial production processes. Enzymatic degradation of these polymers has received attention for many years and is becoming a more and more attractive alternative to chemical and mechanical processes. Over the past 15 years, much progress has been made in elucidating the structural characteristics of these polysaccharides and in characterizing the enzymes involved in their degradation and the genes of biotechnologically relevant microorganisms encoding these enzymes. The members of the fungal genus Aspergillus are commonly used for the production of polysaccharide-degrading enzymes. This genus produces a wide spectrum of cell wall-degrading enzymes, allowing not only complete degradation of the polysaccharides but also tailored modifications by using specific enzymes purified from these fungi. This review summarizes our current knowledge of the cell wall polysaccharide-degrading enzymes from aspergilli and the genes by which they are encoded.

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“…24) However, a higher pH optimum of 5.0 to 6.5 has been reported for the -D-xylosidase from Aspergillus spp. 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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Purification and regulation of the synthesis of a β-xylosidase from Aspergillus nidulans

Cited by 32 publications

References 5 publications

Genetic Evidence for a Defective Xylan Degradation Pathway in Lactococcus lactis

Genetic Evidence for a Defective Xylan Degradation Pathway in Lactococcus lactis

AspergillusEnzymes Involved in Degradation of Plant Cell Wall Polysaccharides

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

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