Xylanolytic enzyme systems in <i>Arthrobacter</i> sp. MTCC 5214 and <i>Lactobacillus</i> sp.

Khandeparker, Rakhee; Jalal, Thasneem

doi:10.1002/bab.1253

Cited by 8 publications

(2 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…MTCC5214 and Lactobacillus sp. based on the elution profile and zymogram analysis [ 13 ], a bifunctional enzyme possessing acetyl xylan esterase and α- l -arabinofuranosidase activities has not been studied in detail, and would be potentially useful for hydrolyzing lignocellulose.…”

Section: Introductionmentioning

confidence: 99%

A novel bifunctional acetyl xylan esterase/arabinofuranosidase from Penicillium chrysogenum P33 enhances enzymatic hydrolysis of lignocellulose

Zhu

Yang

et al. 2017

Microb Cell Fact

View full text Add to dashboard Cite

BackgroundXylan, the major constituent of hemicellulose, is composed of β-(1,4)-linked xylopyranosyl units that for the backbone, with side chains formed by other chemical moieties such as arabinose, galactose, mannose, ferulic acid and acetyl groups. Acetyl xylan esterases and α-l-arabinofuranosidases are two important accessory enzymes that remove side chain residues from xylan backbones and may act in synergy with other xylanolytic enzymes. Compared with enzymes possessing a single catalytic activity, multifunctional enzymes can achieve lignocellulosic biomass hydrolysis using a less complex mixture of enzymes.ResultsHere, we cloned an acetyl xylan esterase (PcAxe) from Penicillium chrysogenum P33 and expressed it in Pichia pastoris GS115. The optimal pH and temperature of the recombinant PcAxe (rPcAxe) for 4-nitrophenyl acetate were 7.0 and 40 °C, respectively. rPcAxe is stable across a broad pH range, retaining 100% enzyme activity om pH 6–9 after a 1 h incubation. The enzyme tolerates the presence of a wide range of metal ions. Sequence alignment revealed a GH62 domain exhibiting α-l-arabinofuranosidase activity with pH and temperature optima of pH 7.0 and 50 °C, in addition to the expected esterase domain. rPcAxe displayed significant synergy with a recombinant xylanase, with a degree of synergy of 1.35 for the hydrolysis of delignified corn stover. Release of glucose was increased by 51% from delignified corn stover when 2 mg of a commercial cellulase was replaced by an equivalent amount of rPcAxe, indicating superior hydrolytic efficiency.ConclusionsThe novel bifunctional enzyme PcAxe was identified in P. chrysogenum P33. rPcAxe includes a carbohydrate esterase domain and a glycosyl hydrolase family 62 domain. This is the first detailed report on a novel bifunctional enzyme possessing acetyl xylan esterase and α-l-arabinofuranosidase activities. These findings expand our current knowledge of glycoside hydrolases and pave the way for the discovery of similar novel enzymes.Electronic supplementary materialThe online version of this article (doi:10.1186/s12934-017-0777-7) contains supplementary material, which is available to authorized users.

show abstract

Section: Introductionmentioning

confidence: 99%

A novel bifunctional acetyl xylan esterase/arabinofuranosidase from Penicillium chrysogenum P33 enhances enzymatic hydrolysis of lignocellulose

Zhu

Yang

et al. 2017

Microb Cell Fact

View full text Add to dashboard Cite

show abstract

“…It was reported that a marine isolate, Lactobacillus sp., showed xylanolytic enzyme activities such as α-Larabinofuranosidase and AXE [18]. However, the related genes and enzymes have not been characterized from lactic acid bacteria yet.…”

Section: Gene Cloning and Expression Of Axesmentioning

confidence: 99%

Functional Expression and Characterization of Acetyl Xylan Esterases CE Family 7 from Lactobacillus antri and Bacillus halodurans

Kim¹,

Jang²,

Nam³

et al. 2020

Journal of Microbiology and Biotechnology

View full text Add to dashboard Cite

Acetyl xylan esterase (AXE; E.C. 3.1.1.72) is one of the accessory enzymes for xylan degradation, which can remove the terminal acetate residues from xylan polymers. In this study, two genes encoding putative AXEs (LaAXE and BhAXE) were cloned from Lactobacillus antri DSM 16041 and Bacillus halodurans C-125, and constitutively expressed in Escherichia coli . They possess considerable activities towards various substrates such as p -nitrophenyl acetate, 4-methylumbelliferyl acetate, glucose pentaacetate, and 7-amino cephalosporanic acid. LaAXE and BhAXE showed the highest activities at pH 7.0 and 8.0 at 50°C, respectively. These enzymes are AXE members of carbohydrate esterase (CE) family 7 with the cephalosporine-C deacetylase activity for the production of antibiotics precursors. The simultaneous treatment of LaAXE with Thermotoga neapolitana β-xylanase showed 1.44-fold higher synergistic degradation of beechwood xylan than the single treatment of xylanase, whereas BhAXE showed no significant synergism. It was suggested that LaAXE can deacetylate beechwood xylan and enhance the successive accessibility of xylanase towards the resulting substrates. The novel LaAXE originated from a lactic acid bacterium will be utilized for the enzymatic production of D-xylose and xylooligosaccharides.

show abstract

Expression and characterisation of a pH and salt tolerant, thermostable and xylose tolerant recombinant GH43 β-xylosidase from Thermobifida halotolerans YIM 90462T for promoting hemicellulose degradation

Yin

Xian

Han

et al. 2018

Antonie van Leeuwenhoek

View full text Add to dashboard Cite

A gene encoding a β-xylosidase (designated as Thxyl43A) was cloned from strain Thermobifida halotolerans YIM 90462. The open reading frame of this gene encodes 550 amino acid residues. The gene was over-expressed in Escherichia coli and the recombinant protein was purified. The monomeric Thxyl43A protein presented a molecular mass of 61.5 kDa. When p-nitrophenyl-β-d-xylopyranoside was used as the substrate, recombinant Thxyl43A exhibited optimal activity at 55 °C and pH 4.0 to 7.0, being thermostable by maintaining 47% of its activity after 30 h incubation at 55 °C. The recombinant enzyme retained more than 80% residual activity after incubation at pH range of 4.0 to 12.0 for 24 h, respectively, which indicated notable thermostability and pH stability of Thxyl43A. Moreover, Thxyl43A displayed high catalytic activity (> 60%) in presence of 5-35% NaCl (w/v) or 1-20% ionic liquid (w/v) or 1-50 mM xylose. These properties suggest that Thxyl43A has potential for promoting hemicellulose degradation and other industrial applications.

show abstract

Xylanolytic enzyme systems in Arthrobacter sp. MTCC 5214 and Lactobacillus sp.

Cited by 8 publications

References 20 publications

A novel bifunctional acetyl xylan esterase/arabinofuranosidase from Penicillium chrysogenum P33 enhances enzymatic hydrolysis of lignocellulose

A novel bifunctional acetyl xylan esterase/arabinofuranosidase from Penicillium chrysogenum P33 enhances enzymatic hydrolysis of lignocellulose

Functional Expression and Characterization of Acetyl Xylan Esterases CE Family 7 from Lactobacillus antri and Bacillus halodurans

Expression and characterisation of a pH and salt tolerant, thermostable and xylose tolerant recombinant GH43 β-xylosidase from Thermobifida halotolerans YIM 90462T for promoting hemicellulose degradation

Contact Info

Product

Resources

About