Enzymatic characterization of a novel thermostable and alkaline tolerant GH10 xylanase and activity improvement by multiple rational mutagenesis strategies

Lai, Zhihua; Zhou, Cheng; Ma, Xiaochen; Xue, Yanfen; Ma, Yanhe

doi:10.1016/j.ijbiomac.2020.12.137

Cited by 22 publications

(21 citation statements)

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“…Another novel thermostable xylanase from Chaetomium showed less than 70% activity after 30 min incubation under 70 °C 50 . In another study, a thermostable and alkaline tolerant xylanase from Bacillus was completely inactivated after 10 min incubation at 70 °C 51 . Comparing the thermal stability of the PersiXyn8 with previously reported xylanases proved another important property of the enzyme for industrial purposes.…”

Section: Discussionmentioning

confidence: 99%

In vitro bioprocessing of corn as poultry feed additive by the influence of carbohydrate hydrolyzing metagenome derived enzyme cocktail

Mousavi

Motahar

Salami

et al. 2022

Sci Rep

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The carbohydrate-hydrolyzing enzymes play a crucial role in increasing the phenolic content and nutritional properties of polysaccharides substrate, essential for cost-effective industrial applications. Also, improving the feed efficiency of poultry is essential to achieve significant economic benefits. The current study introduced a novel thermostable metagenome-derived xylanase named PersiXyn8 and investigated its synergistic effect with previously reported α-amylase (PersiAmy3) to enhance poultry feed utilization. The potential of the enzyme cocktail in the degradation of poultry feed was analyzed and showed 346.73 mg/g poultry feed reducing sugar after 72 h of hydrolysis. Next, the impact of solid-state fermentation on corn quality was investigated in the presence and absence of enzymes. The phenolic content increased from 36.60 mg/g GAE in control sample to 68.23 mg/g in the presence of enzymes. In addition, the enzyme-treated sample showed the highest reducing power OD 700 of 0.217 and the most potent radical scavenging activity against ABTS (40.36%) and DPPH (45.21%) radicals. Moreover, the protein and ash contents of the fermented corn increased by 4.88% and 6.46%, respectively. These results confirmed the potential of the carbohydrate-hydrolyzing enzymes cocktail as a low-cost treatment for improving the phenolic content, antioxidant activity, and nutritional values of corn for supplementation of corn-based poultry feed.

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Section: Discussionmentioning

confidence: 99%

In vitro bioprocessing of corn as poultry feed additive by the influence of carbohydrate hydrolyzing metagenome derived enzyme cocktail

Mousavi

Motahar

Salami

et al. 2022

Sci Rep

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“…SN5 [ 9 ], Xyn30Y5 of Bacillus sp. 30Y5 [ 13 ], and r-XynA of Sorangium cellulosum So9733-1 [ 31 ] were optimally active at neutral pH, while iXylC of Cohnella laeviribosi HY-21 [ 32 ], Xyn10A of Flavobacterium johnsoniae [ 33 ], CbXyn10B of Caldicellulosiruptor bescii [ 34 ], and XynDZ5 of Thermoanaerobacterium sp. [ 35 ] were at slightly alkaline pH (7.5–8.0) ( Table 1 ).…”

Section: Resultsmentioning

confidence: 99%

“…rXynAHJ2 of Bacillus sp. HJ2 [ 10 ] and Xyn30Y5 [ 13 ] exhibited over 50% and 80% residual activity, respectively, when incubated at a pH range of 6.0–10.0, but at different incubation conditions ( Table 1 ).…”

Section: Resultsmentioning

confidence: 99%

“…Xyn10 [ 8 ], Xyn10A of Bacillus sp. SN5 [ 9 ], Xyn30Y5 [ 13 ], r-XynA [ 31 ], and Xyn10A of F. johnsoniae [ 33 ] were also active on different xylans with no activity toward glucose–based polysaccharides, while the XynA of Bacillus sp. KW1 [ 12 ], iXylC [ 32 ], and CbXyn10B [ 34 ] exhibited activity toward CMC and aryl-glycosides.…”

Section: Resultsmentioning

confidence: 99%

“…Bacteria have an advantage over fungi for xylanase production as the optimum pH for bacterial xylanases lies in the neutral or alkaline range, whereas for fungal xylanases, it is in the acidic range [ 4 ]. Among the xylanolytic microorganisms, Gram-positive Bacillus tends to be marked as a significant industrial workhorse due to its fast growth and innate capacity to produce large amounts of extracellular enzymes [ 8 , 9 , 10 , 11 , 12 , 13 ].…”

Section: Introductionmentioning

confidence: 99%

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Biochemical and Thermodynamic Studies on a Novel Thermotolerant GH10 Xylanase from Bacillus safensis

et al. 2022

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Xylanases have a broad range of applications in agro-industrial processes. In this study, we report on the discovery and characterization of a new thermotolerant GH10 xylanase from Bacillus safensis, designated as BsXyn10. The xylanase gene (bsxyn10) was cloned from Bacillus safensis and expressed in Escherichia coli. The reduced molecular mass of BsXyn10 was 48 kDa upon SDS-PAGE. Bsxyn10 was optimally active at pH 7.0 and 60 °C, stable over a broad range of pH (5.0–8.0), and also revealed tolerance toward different modulators (metal cations, EDTA). The enzyme was active toward various xylans with no activity on the glucose-based polysaccharides. KM, vmax, and kcat for oat spelt xylan hydrolysis were found to be 1.96 g·L−1, 58.6 μmole·min−1·(mg protein)−1, and 49 s−1, respectively. Thermodynamic parameters for oat spelt xylan hydrolysis at 60 °C were ΔS* = −61.9 J·mol−1·K−1, ΔH* = 37.0 kJ·mol−1 and ΔG* = 57.6 kJ·mol−1. BsXyn10 retained high levels of activity at temperatures up to 60 °C. The thermodynamic parameters (ΔH*D, ΔG*D, ΔS*D) for the thermal deactivation of BsXyn10 at a temperature range of 40–80 °C were: 192.5 ≤ ΔH*D ≤ 192.8 kJ·mol−1, 262.1 ≤ ΔS*D ≤ 265.8 J·mol−1·K−1, and 99.9 ≤ ΔG*D ≤ 109.6 kJ·mol−1. The BsXyn10-treated oat spelt xylan manifested the catalytic release of xylooligosaccharides of 2–6 DP, suggesting that BsXyn10 represents a promising candidate biocatalyst appropriate for several biotechnological applications.

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Enhancing the thermostability and catalytic activity of Bacillus subtilis chitosanase by saturation mutagenesis of Lys242

Guo,

Gao,

Zhang

et al. 2023

Biotechnology Journal

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Catalysis activity and thermostability are some of the fundamental characteristic of enzymes, which are of great significance to their industrial applications. Bacillus subtilis chitosanase BsCsn46A is a kind of enzyme with good catalytic activity and stability, which can hydrolyze chitosan to produce chitobiose and chitotriose. In order to further improve the catalytic activity and stability of BsCsn46A, saturation mutagenesis of the C‐terminal K242 of BsCsn46A was performed. The results showed that the six mutants (K242A, K242D, K242E, K242F, K242P and K242T) showed increased catalytic activity on chitosan. The catalytic activity of K242P increased from 12971 ± 597 U/mg of wild type to 17820 ± 344 U/mg, and the thermostability of K242P increased by 2.27%. In order to elucidate the reason for the change of enzymatic properties, hydrogen network, molecular docking and molecular dynamics simulation were carried out. The hydrogen network results showed that all the mutants lose their interaction with Asp6 at 242 site, thereby increasing the flexibility of Glu19 at the junction sites of α1 and loop1. Molecular dynamics results showed that the RMSD of K242P was lower at both 313 and 323 K than that of other mutants, which supported that K242P had better thermostability. The catalytic activity of mutant K242P reached 17820.27 U/mg, the highest level reported so far, which could be a robust candidate for the industrial application of chitooligosaccharide (COS) production.This article is protected by copyright. All rights reserved

show abstract

Enzymatic characterization of a novel thermostable and alkaline tolerant GH10 xylanase and activity improvement by multiple rational mutagenesis strategies

Cited by 22 publications

References 94 publications

In vitro bioprocessing of corn as poultry feed additive by the influence of carbohydrate hydrolyzing metagenome derived enzyme cocktail

In vitro bioprocessing of corn as poultry feed additive by the influence of carbohydrate hydrolyzing metagenome derived enzyme cocktail

Biochemical and Thermodynamic Studies on a Novel Thermotolerant GH10 Xylanase from Bacillus safensis

Enhancing the thermostability and catalytic activity of Bacillus subtilis chitosanase by saturation mutagenesis of Lys242

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