Interlaboratory testing of methods for assay of xylanase activity

Bailey, Michael; Biely, Peter; Poutanen, Kaisa

doi:10.1016/0168-1656(92)90074-j

Cited by 2,171 publications

(977 citation statements)

References 18 publications

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“…The liberation of reducing sugars was estimated by the dinitrosalicylic acid method [25] using xylose as a standard. Reducing sugars were determined by measuring the absorption at 540 nm relative to a D-xylose standard.…”

Section: Xylanase Activity Assaysmentioning

confidence: 99%

“…And the catalysis area of xylanase has the high homology in the same family. Xylanases of family GH11 are mostly single domains with a relatively low molecular weight (MW) (19)(20)(21)(22)(23)(24)(25), the optimum temperature 50-60°C and a b-jelly roll structure compared to the family F/10 xylanases that are more domains, not only the catalytic domain, but also cellulose binding domain, with a high MW ([30 kDa), the optimum temperature 60-80°C and a (ab) 8 barrel structure [4,10]. The major enzymes comprising the GH10 family are endo-1,4-b-xylanases and a small number of endo-1,3-b-xylanases (EC 3.2.1.32).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S

Wang

et al. 2012

Indian J Microbiol

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A xylanase gene (xynZF-2) from the Aspergillus niger XZ-3S was cloned and expressed in Escherichia coli. The coding region of the gene was separated by only one intron with the 68 bp in length. It encoded 225 amino acid residues of a protein with a calculated molecular weight of 24.04 kDa plus a signal peptide of 18 amino acids. The amino acid sequence of the xynZF-2 gene had a high similarity with those of family 11 of glycosyl hydrolases reported from other microorganisms. The mature peptide encoding cDNA was subcloned into pET28a(?) expression vector. The resultant recombinant plasmid pET-28a-xynZF-2 was transformed into E. coli BL21(DE3), and finally the recombinant strain BL21/xynZF-2 was obtained. A maximum activity of 42.33 U/mg was gained from cellular of E. coli BL21/xynZF-2 induced by IPTG. The optimum temperature and pH for recombinant enzyme which has a good stability in alkaline conditions were 40°C and 5.0, respectively. Fe 3? had an active effect on the enzyme obviously.

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Section: Xylanase Activity Assaysmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S

Wang

et al. 2012

Indian J Microbiol

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“…The extracts were centrifuged and stored at 4 °C. The xylanases activity was determined by the amount of reducing sugars released from xylan "birchwood" as described by Bailey et al (1992). The enzymatic assay was carried for 5 minutes, 0.9 mL of 1% xylan along with 0.1 mL of enzyme extract, the reducing sugars were measured by the method of 3,5 dinitrosalicylic (DNS) (Miller, 1959).…”

Section: Enzymatic Activitiesmentioning

confidence: 99%

Influence of nitrogen sources on the enzymatic activity and grown by Lentinula edodes in biomass Eucalyptus benthamii

et al. 2015

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Lignocellulose is the most abundant environmental component and a renewable organic resource in soil. There are some filamentous fungi which developed the ability to break down and use cellulose, hemicellulose and lignin as an energy source. The objective of this research was to analyze the effect of three nitrogen resources (ammonium sulfate, saltpetre, soybean) in the holocellulolitic activity of Lentinula edodes EF 50 using as substrate sawdust E. benthamii. An experimental design mixture was applied with repetition in the central point consisting of seven treatments (T) of equal concentrations of nitrogen in ammonium sulfate, potassium nitrate and soybean. The enzymatic activity of avicelase, carboxymetilcellulase, β-glucosidase, xylanases and manganese peroxidase was determined. The humidity, pH, water activity (a w ) and qualitative analysis of mycelial growth in 8 times of cultivation were evaluated. The results showed negative effect on enzyme production in treatments with maximum concentration of ammonium sulfate and potassium nitrate. The treatments with cooked soybean flour expressed higher enzymatic activities in times of 3, 6 and 9 days of culture, except in the activity of manganese peroxidase. The highest production was observed in the treatment with ammonium sulfate, and soybean (83.86 UI.L -1 ) at 20 days of cultivation.

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“…Cellulase activity was reported in filter paper units. Xylanase activity was measured by using oat spelt xylan (Bailey et al, 1992), whereas CMC activity was estimated by using the method given by Mandels et al (1974). One unit of enzyme (CMC, FPU, and xylanase) is defined as one micro mol production of glucose/xylose per ml per minute.…”

Section: Methodsmentioning

confidence: 99%

NaOH Pretreatment and Enzymatic Hydrolysis ofSaccharum spontaneumfor Reducing Sugars Production

Kataria

Ghosh

2014

Energy Sources, Part A: Recovery, Utilization, and Environmenta

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Ethanol from lignocellulosic material is the second generation biofuel production, which includes different initial steps of pretreatment and hydrolysis to form fermentable sugars. The aim of this study was to utilize Saccharum spontaneum (Kans grass, a perennial grass) for NaOH pretreatment and further hydrolysis with on-site produced cellulase enzyme that minimizes the cost of the overall process of bioethanol synthesis. Five percent (w/v) Kans grass was first pretreated with different concentrations of NaOH (0.5, 1. 1.5, and 2% w/v) at variable durations of time period (30, 60, 90, and 120 min) at 121 ı C. The pretreated biomass was further supplied with a crude mixture of cellulase enzyme (20 units/g biomass) obtained from Trichoderma reesei for saccharification. The crude mixture of enzyme is composed with CMCase, FPAse, and xylanase activities 1.41, 1.12, and 6.23, respectively. The best condition for total reducing sugars (350 mg/g) was found to be at 0.5% NaOH with 120 ı C where 70.75% of lignin removal was obtained and holocellulose (total carbohydrate) content was increased from 64.7 to 79.61%.

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Interlaboratory testing of methods for assay of xylanase activity

Cited by 2,171 publications

References 18 publications

Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S

Cloning, Expression, and Characterization of an GHF 11 Xylanase from Aspergillus niger XZ-3S

Influence of nitrogen sources on the enzymatic activity and grown by Lentinula edodes in biomass Eucalyptus benthamii

NaOH Pretreatment and Enzymatic Hydrolysis ofSaccharum spontaneumfor Reducing Sugars Production

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