Microbial xylanases and their biomedical applications: a review

Goswami, Girish K; Pathak, Rakesh R.

doi:10.5455/2319-2003.ijbcp20130602

Cited by 28 publications

(11 citation statements)

References 78 publications

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“…The GH11 families are the smallest xylanases (generally less than 30 kDa), which penetrate into the pulp easily with high specificity, but do not tolerate high temperature4. Previously, many efforts have been reported to improve the thermo-stability of xylanases by different strategies56. N-terminal region of xylanase was reported to play a crucial role in its thermo-stability, so single residue substitutions and chimeric alterations in the vicinity of the N-terminal region of the protein make a big difference789.…”

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confidence: 99%

High-level expression of improved thermo-stable alkaline xylanase variant in Pichia Pastoris through codon optimization, multiple gene insertion and high-density fermentation

Fang

Wang

et al. 2016

Sci Rep

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In paper industry, xylanases are used to increase the pulp properties in bleaching process as its eco-friendly nature. The xylanases activity is hindered by high temperature and alkaline conditions with high enzyme production cost in the paper industry. Here, XynHB, an alkaline stable xylanase from Bacillus pumilus HBP8 was mutated at N188A to XynHBN188A. Expressed mutant in E. coli showed 1.5-fold higher xylanase activity than XynHB at 60 °C. The mutant expressed in Pichia pastoris was glycosylated, remained stable for 30 min at 60 °C. XynHBN188A optimized based on codon usage bias for P. pastoris (xynHBN188As) showed an increase of 39.5% enzyme activity. The strain Y16 forming the largest hydrolysis halo in the xylan plate was used in shake flask experiments produced an enzyme activity of 6,403 U/ml. The Y16 strain had 9 copies of the recombinant xynHBN188As gene in the genome revealed by qPCR. The enzymatic activity increased to 48,241 U/ml in a 5 L fermentor. Supplement of 15 U/g xylanase enhanced the brightness of paper products by 2% in bleaching experiment, and thereby improved the tensile strength and burst factor by 13% and 6.5%, respectively. XynHBN188As has a great potential in paper industries.

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confidence: 99%

High-level expression of improved thermo-stable alkaline xylanase variant in Pichia Pastoris through codon optimization, multiple gene insertion and high-density fermentation

Fang

Wang

et al. 2016

Sci Rep

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“…Therefore, the presence of xylanases in the enzymatic cocktail is very important to disrupt xylan and to facilitate the access of cellulases to their substrate, when the objective is to obtain glucose from this cellulose, in the context of sugarcane bagasse saccharification for second generation ethanol production (Kalim et al, 2015). Both cellulases and xylanases can be used in several other industrial processes, highlighting the textile, pulping, and animal nutrition sectors (Goswami and Rawat, 2015;Kuhad et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

Cellulases and xylanases production by endophytic fungi by solid state fermentation using lignocellulosic substrates and enzymatic saccharification of pretreated sugarcane bagasse

Marques

Pereira

Gomes

et al. 2018

Industrial Crops and Products

115

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A B S T R A C TEndophytic fungi are widely studied as producers of secondary metabolites of biotechnological interest. In recent years, the interest in these fungi as new sources of enzymes, especially hydrolytic, has increased. In the present study, 14 strains of endophytic fungi not yet explored as enzymes sources were randomly chosen and prospected for cellulases and xylanases production by solid-state fermentation. Initially, fungi were cultivated in a mixture (1:1 w/w) of sugarcane bagasse and wheat bran for 7 days, at 28°C. In this initial screening, 4 fungi excelled in endoglucanase activity (U/g): Cladosporium cladosporioides PAJ 03 (88.51 ± 1.0), Phomopsis stipata SC 04 (83.44 ± 7.7), Trichoderma viridae PAJ 01 (64.56 ± 4.0) and Botryosphaeria sp. AM 01 (42.79 ± 1.6). On the other hand, the following 4 fungi stood out in relation to β-glucosidase activity (U/g): Saccharicola sp. EJC 04 (51.56 ± 2.7), Paecilomyces sp. SF 021 (33.19 ± 9.2), Ustilaginoidea sp. CV 04 (29.75 ± 0.8) and Ustilaginoidea sp. XYA 04 (21.72 ± 3.05). Among these fungi, P. stipata SC 04 and Botryosphaeria sp. AM 01 were the best producers of xylanase and β-xilosidase (694,33 and 4,87 U/g, respectively). These 8 fungi were then cultured in new mixtures (1:1 w/w) of lignocellulosic substrates. Botryosphaeria sp. AM01and Saccharicola sp. EJC04 stood out regarding endoglucanase and β-glucosidase activities (184.74 ± 6.0 and 92.28 ± 9.57 U/g, respectively) when cultivated on cotton seed meal and wheat bran and were selected to continue the study. The influence of time cultivation, inoculum amount and substrate initial moisture content was evaluated and the best condition for cellulases production was 192 h, six mycelial plugs and 65%, respectively, for both fungi. Cellulases and xylanases produced under these conditions were characterized and optimum pH and temperature values were between 4.5-6 and 60-75°C, respectively. The enzymes were stable over a wide pH range and under 30-70°C. β-glucosidase from both isolates retained about 75-80% of their activity in the presence of glucose at 6 mM. The presence of ethanol stimulated β-glucosidase activity from Botryosphaeria sp. AM01 (about 60% higher in the presence of ethanol at 15%). On the other hand, the activity of β-glucosidase produced by Saccharicola sp. EJC 04 was reduced at ethanol concentrations above 15%. A blend of the enzymatic extracts was used to saccharify pretreated sugarcane bagasse and a face-centered central composite design was used to find the best conditions. Under the predicted optimum condition (50°C, 5% of sugarcane bagasse, 150 U g −1 of endoglucanase and 20 h), glucose and xylose concentrations obtained were 3.56 and 1.66 mg mL −1 , respectively. These results show that the 14 endophytic fungi studied have potential to be explored as producers of plant material degrading enzymes. Botryosphaeria sp. AM01 and Saccharicola sp. EJC 04 are promising in relation

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“…Additional to industrial use of xylanase in kraft pulp production, thermostable xylanase has wider application in fishery, piggery, cattle food and human food 12 . The present study describes partial purification and characterization of a termostable xylanase from Bacillus brevis grown on wheat straw as substrate.…”

Section: Introductionmentioning

confidence: 99%

Production, Partial Purification and Biochemical Characterization of Thermostable Xylanase from Bacillus brevis

Goswami¹,

Pathak²,

Krishnamohan³

et al. 2013

Biomed. Pharmacol. J.

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Microbial xylanases and their biomedical applications: a review

Cited by 28 publications

References 78 publications

High-level expression of improved thermo-stable alkaline xylanase variant in Pichia Pastoris through codon optimization, multiple gene insertion and high-density fermentation

High-level expression of improved thermo-stable alkaline xylanase variant in Pichia Pastoris through codon optimization, multiple gene insertion and high-density fermentation

Cellulases and xylanases production by endophytic fungi by solid state fermentation using lignocellulosic substrates and enzymatic saccharification of pretreated sugarcane bagasse

Production, Partial Purification and Biochemical Characterization of Thermostable Xylanase from Bacillus brevis

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