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

Glekas, Panayiotis D.; Kalantzi, Styliani; Dalios, Anargiros; Hatzinikolaou, Dimitris G.; Mamma, Diomi

doi:10.3390/biom12060790

Cited by 11 publications

(8 citation statements)

References 43 publications

(103 reference statements)

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“…[21, 22] and others have been used to produce xylanase. Many parameters, such as temperature, pH, metal ions, detergents and others, affect the activities of xylanase [3, 16].…”

Section: Introductionmentioning

confidence: 99%

“…Many micro-organisms such as Bacillus spp. [3, 7, 12, 13], Aspergillus spp. [14–16], Penicillium spp.…”

Section: Introductionmentioning

confidence: 99%

“…Lignocellulosic materials are abundant in nature and are principally made up of cellulose, hemicellulose and lignin [1, 2]. Hemicellulose is the second most plentiful biological polymer in the world after cellulose and the main component of hemicellulose is xylan, which is broken down to xylose by the enzyme called xylanase [3]. Xylanase is a hydrolytic enzyme that breaks the β−1, 4-glycosidic bond of xylan in lignocellulolytic substrates to release xylose.…”

Section: Introductionmentioning

confidence: 99%

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Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation

Fasiku

Bello

Odeniyi

2023

Access Microbiology

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Xylanase breaks xylan down to xylose, which is used in industries such as pulp and paper, food and feed, among others. The utilization of wastes for xylanase production is economical, hence this work aimed at producing xylanase through solid-state fermentation and characterizing the enzyme. Xylanase-producing strains of Bacillus megaterium and Aspergillus niger GIO were inoculated separately in a 5 and 10 day solid fermentation study on maize straw, rice straw, sawdust, corn cob, sugarcane bagasse, conifer litters, alkaline-pretreated maize straw (APM) and combined alkaline and biological-pretreated maize straw, respectively. The best substrate was selected for xylanase production. The crude enzyme was extracted from the fermentation medium and xylanase activity was characterized using parameters such as temperature, cations, pH and surfactants. Among different substrates, the highest xylanase activity of 3.18 U ml−1 was recorded when A. niger GIO was grown on APM. The xylanase produced by A. niger GIO and B. megaterium had the highest activities (3.67 U ml−1 and 3.36 U ml−1) at 40 °C after 30 and 45 min of incubation, respectively. Optimal xylanase activities (4.58 and 3.58 U ml−1) of A. niger GIO and B. megaterium , respectively, were observed at pH 5.0 and 6.2. All cations used enhanced xylanase activities except magnesium ion. Sodium dodecyl sulfate supported the highest xylanase activity of 6.13 and 6.90 U ml−1 for A. niger GIO and B. megaterium , respectively. High yields of xylanase were obtained from A. niger GIO and B. megaterium cultivated on APM. The xylanase activities were affected by pH, temperature, surfactants and cations.

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“…[21, 22] and others have been used to produce xylanase. Many parameters, such as temperature, pH, metal ions, detergents and others, affect the activities of xylanase [3, 16].…”

Section: Introductionmentioning

confidence: 99%

“…Many micro-organisms such as Bacillus spp. [3, 7, 12, 13], Aspergillus spp. [14–16], Penicillium spp.…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation

Fasiku

Bello

Odeniyi

2023

Access Microbiology

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“…The results showed that XYNF1-AS had K m of 7.41 mg mL −1 and k cat of 19.51 min −1 . XYNF1-AS did not display superior catalytic properties compared to known GH10 xylanases (Glekas et al 2022 ; Lafond et al 2011 ; You et al 2019 ).…”

Section: Resultsmentioning

confidence: 95%

Alternative splicing analysis of lignocellulose-degrading enzyme genes and enzyme variants in Aspergillus niger

Xu,

Dong,

Wang

et al. 2024

Appl Microbiol Biotechnol

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Alternative splicing (AS) greatly expands the protein diversity in eukaryotes. Although AS variants have been frequently reported existing in filamentous fungi, it remains unclear whether lignocellulose-degrading enzyme genes in industrially important fungi undergo AS events. In this work, AS events of lignocellulose-degrading enzymes genes in Aspergillus niger under two carbon sources (glucose and wheat straw) were investigated by RNA-Seq. The results showed that a total of 23 out of the 56 lignocellulose-degrading enzyme genes had AS events and intron retention was the main type of these AS events. The AS variant enzymes from the annotated endo-β-1,4-xylanase F1 gene (xynF1) and the endo-β-1,4-glucanase d gene (eglD), noted as XYNF1-AS and EGLD-AS, were characterized compared to their normal splicing products XYNF1 and EGLD, respectively. The AS variant XYNF1-AS displayed xylanase activity whereas XYNF1 did not. As for EGLD-AS and EGLD, neither of them showed annotated endo-β-1,4-glucanase activity. Instead, both showed lytic polysaccharide monooxygenase (LPMO) activity with some differences in catalytic properties. Our work demonstrated that the AS variants in A. niger were good sources for discovering novel lignocellulose-degrading enzymes. Key points • AS events were identified in the lignocellulose-degrading enzyme genes of A. niger. • New β-1,4-xylanase and LPMO derived from AS events were characterized.

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“…The temperature coefficient value (Q 10 ) for optimal temperatures of free Xyl, Xyl@ZIF-67, and Xyl@Mn/ZIF-67 was calculated via the following Eq. 2 [35].…”

Section: Determination Of Optimum Temperature and Phmentioning

confidence: 99%

Immobilization of Xylanase into Zeolitic Imidazolate Framework-67 (ZIF-67) and Manganese-Doped ZIF-67 (Mn/ZIF-67): A Comparison Study

Bakar,

Dik,

Ulu

et al. 2024

Top Catal

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It has been discovered that metal–organic frameworks (MOFs) have desirable qualities for the immobilization of enzymes, including a high surface area, significant interior pore volumes, and easily changeable pore size. Herein, the xylanase (Xyl) enzyme was immobilized for the first time to two different carrier supports, zeolitic imidazolate framework-67 (ZIF-67) and manganese-doped ZIF-67 (Mn/ZIF-67) by in situ method. The physicochemical characterizations of MOFs with and without Xyl were performed by FT-IR, XRD, SEM, and EDAX techniques. Xyl@ZIF-67 and Xyl@Mn/ZIF-67 were evaluated in terms of optimum temperature, optimum pH, kinetic parameters, thermal stability, reusability as well as juice clarification and compared with free Xyl. Optimum temperature values were 50 °C for Xyl@ZIF-67 and 70 °C for free Xyl and Xyl@Mn/ZIF-67. Optimum pH values for free Xyl, Xyl@ZIF-67, and Xyl@Mn/ZIF-67 were recorded as 6.0, 8.0, and 7.0, respectively. Km values for free Xyl, Xyl@ZIF-67, and Xyl@Mn/ZIF-67 were calculated as 3.139, 5.430, and 0.799 mg/mL, respectively, while Vmax values were calculated as 0.167, 0.226, and 0.062 µmol/min/mL, respectively. The results revealed that in comparison to the free Xyl, Xyl@ZIF-67, and Xyl@Mn/ZIF-67 exhibited more thermal resistance. After incubation at 70 °C for 120 min, the free Xyl remained at 28.7% of the activity, while the Xyl@ZIF-67 and Xyl@Mn/ZIF-67 remained at 85.7% and 40.0%, respectively. Moreover, after eight cycles, the Xyl@ZIF-67 and Xyl@Mn/ZIF-67 retained more than 70% of their initial activity. Further, the transmittance of apple juice was increased from 65.61 to 94.73% and from 77.80 to 84.13%, respectively, when Xyl@ZIF-67 and Xyl@Mn/ZIF-67 were used as biocatalysts. Overall, these findings indicated that the suggested Xyl@ZIF-67 and Xyl@Mn/ZIF-67 have a high potential for juice clarification as an efficient heterogeneous biocatalyst. Graphical Abstract

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

Cited by 11 publications

References 43 publications

Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation

Production of xylanase by Aspergillus niger GIO and Bacillus megaterium through solid-state fermentation

Alternative splicing analysis of lignocellulose-degrading enzyme genes and enzyme variants in Aspergillus niger

Immobilization of Xylanase into Zeolitic Imidazolate Framework-67 (ZIF-67) and Manganese-Doped ZIF-67 (Mn/ZIF-67): A Comparison Study

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