Biochemical characterization of a novel halo/organic-solvents/final-products tolerant GH39 xylosidase from saline soil and its synergic action with xylanase

Li, Zhongyuan; Chen, Shiheng; Wang, Yan; Liu, Zhongqi; Xia, Zhongqiang; Zhang, Minghui; Luo, Xue‐Gang; Song, Yajian; Zhao, Junqi; Zhang, Tongcun

doi:10.1016/j.ijbiomac.2020.07.079

Cited by 9 publications

(8 citation statements)

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“…The relationship between the polarity of solvents and enzyme activity has been highlighted previously [ 51 ]. It has also been noted that increased or reduced structural flexibility of enzymes is primarily responsible for the stimulation or inhibition of enzymatic activities, respectively, in organic solvents [ 52 ]. Hence, it is posited that the xylanase from B. bassiana SAN01 may contain a high proportion of random coils, thus increasing the structural flexibility, which might be responsible for its significant stability in some organic solvents.…”

Section: Resultsmentioning

confidence: 99%

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Amobonye

Bhagwat

Singh

2021

JoF

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Beauveria bassiana is an entomopathogenic fungus widely used as a biopesticide for insect control; it has also been shown to exist as an endophyte, promoting plant growth in many instances. This study highlights an alternative potential of the fungus; in the production of an industrially important biocatalyst, xylanase. In this regard, Beauveria bassiana SAN01 xylanase was purified to homogeneity and subsequently characterized. The purified xylanase was found to have a specific activity of 324.2 Umg−1 and an estimated molecular mass of ~37 kDa. In addition, it demonstrated optimal activity at pH 6.0 and 45 °C while obeying Michaelis–Menton kinetics towards beechwood xylan with apparent Km, Vmax and kcat of 1.98 mgmL−1, 6.65 μM min−1 and 0.62 s−1 respectively. The enzyme activity was strongly inhibited by Ag2+ and Fe3+ while it was significantly enhanced by Co2+ and Mg2+. Furthermore, the xylanase was shown to effectively deink wastepaper at an optimal rate of 106.72% through its enzymatic disassociation of the fiber-ink bonds as demonstrated by scanning electron microscopy and infrared spectroscopy. This is the first study to demonstrate the biotechnological application of a homogeneously purified glycosyl hydrolase from B. bassiana.

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Section: Resultsmentioning

confidence: 99%

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Amobonye

Bhagwat

Singh

2021

JoF

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“…CcXynB2 activity was reduced (33%) when incubated with 2 mM Mn 2+ while the Geobacillus WSUCF-1 enzyme showed no improved activity when assayed at 1 mM Mn 2+ . For JB13GH39 Cu 2+ had a positive effect on activity as did Mn 2+ with a 15% improvement while for Xyl21 both these metal ions reduced activity [ 23 , 42 ]. The large negative electrostatic potential observed for the active sites of these enzymes should attract positively charged ions [ 31 ].…”

Section: Resultsmentioning

confidence: 99%

“…β-xylosidases belong to several glycoside hydrolase families (GH3, GH30, GH39, GH43, GH53, GH54, GH116 and GH120) with all of them functioning as retaining hydrolases except the GH43 family which are inverting enzymes [ 18 ]. Only 12 GH39 β-xylosidases enzymes present in the CAZY database have been characterized and of these few have been identified through metagenomic screens [ 19 – 23 ], making these rather rare enzymes. Patenting of at least one of these enzymes suggest some usefulness in certain applications (WO/2018/185150).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a highly xylose tolerant β-xylosidase isolated from high temperature horse manure compost

et al. 2021

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Background There is a continued need for improved enzymes for industry. β-xylosidases are enzymes employed in a variety of industries and although many wild-type and engineered variants have been described, enzymes that are highly tolerant of the products produced by catalysis are not readily available and the fundamental mechanisms of tolerance are not well understood. Results Screening of a metagenomic library constructed of mDNA isolated from horse manure compost for β-xylosidase activity identified 26 positive hits. The fosmid clones were sequenced and bioinformatic analysis performed to identity putative β-xylosidases. Based on the novelty of its amino acid sequence and potential thermostability one enzyme (XylP81) was selected for expression and further characterization. XylP81 belongs to the family 39 β-xylosidases, a comparatively rarely found and characterized GH family. The enzyme displayed biochemical characteristics (KM—5.3 mM; Vmax—122 U/mg; kcat—107; Topt—50 °C; pHopt—6) comparable to previously characterized glycoside hydrolase family 39 (GH39) β-xylosidases and despite nucleotide identity to thermophilic species, the enzyme displayed only moderate thermostability with a half-life of 32 min at 60 °C. Apart from acting on substrates predicted for β-xylosidase (xylobiose and 4-nitrophenyl-β-D-xylopyranoside) the enzyme also displayed measurable α-L-arabainofuranosidase, β-galactosidase and β-glucosidase activity. A remarkable feature of this enzyme is its ability to tolerate high concentrations of xylose with a Ki of 1.33 M, a feature that is highly desirable for commercial applications. Conclusions Here we describe a novel β-xylosidase from a poorly studied glycosyl hydrolase family (GH39) which despite having overall kinetic properties similar to other bacterial GH39 β-xylosidases, displays unusually high product tolerance. This trait is shared with only one other member of the GH39 family, the recently described β-xylosidases from Dictyoglomus thermophilum. This feature should allow its use as starting material for engineering of an enzyme that may prove useful to industry and should assist in the fundamental understanding of the mechanism by which glycosyl hydrolases evolve product tolerance.

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“…The molecular characteristics involved in the high structural flexibility of salt-tolerant enzymes include the following: (I) At the level of the primary structure, a high proportion of small amino acids is observed for salt-tolerant xylanases . Small amino acids have small side chain groups, which can reduce the interactions among the residues, subsequently leading to a total increase of structural flexibility. , (II) At the secondary structure level, a high percentage of random coil structures at the expense of α-helices is observed in salt-tolerant xylanases. , Random coil structures possess a higher structural flexibility than α-helices and, thus, enhance the overall flexibility. , (III) At the tertiary structure level, salt-tolerant xylanases have fewer salt bridges and hydrogen bonds than their counterparts . The decreased non-covalent bonds in the protein structure are considered beneficial for the conversion to different enzyme conformations, thus leading to increased structural flexibility. , …”

Section: Salt Tolerance Mechanisms Of Xylanasesmentioning

confidence: 99%

Biotechnological Aspects of Salt-Tolerant Xylanases: A Review

Cao

Zhang

Zhou

et al. 2021

J. Agric. Food Chem.

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β-1,4-Xylan is the main component of hemicelluloses in land plant cell walls, whereas β-1,3-xylan is widely found in seaweed cell walls. Complete hydrolysis of xylan requires a series of synergistically acting xylanases. High-saline environments, such as saline–alkali lands and oceans, frequently occur in nature and are also involved in a broad range of various industrial processes. Thus, salt-tolerant xylanases may contribute to high-salt and marine food processing, aquatic feed production, industrial wastewater treatment, saline–alkali soil improvement, and global carbon cycle, with great commercial and environmental benefits. This review mainly introduces the definition, sources, classification, biochemical and molecular characteristics, adaptation mechanisms, and biotechnological applications of salt-tolerant xylanases. The scope of development for salt-tolerant xylanases is also discussed. It is anticipated that this review would serve as a reference for further development and utilization of salt-tolerant xylanases and other salt-tolerant enzymes.

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Biochemical characterization of a novel halo/organic-solvents/final-products tolerant GH39 xylosidase from saline soil and its synergic action with xylanase

Cited by 9 publications

References 25 publications

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Beauveria bassiana Xylanase: Characterization and Wastepaper Deinking Potential of a Novel Glycosyl Hydrolase from an Endophytic Fungal Entomopathogen

Characterization of a highly xylose tolerant β-xylosidase isolated from high temperature horse manure compost

Biotechnological Aspects of Salt-Tolerant Xylanases: A Review

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