Immobilization of mutated xylanase from Neocallimastix patriciarum in E. coli and application for kraft pulp biobleaching

Huang, Ying; Zhang, N.-J.; Zhao, Zhong

doi:10.1590/1519-6984.243629

Cited by 5 publications

(3 citation statements)

References 35 publications

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“…Xylanase enzyme optimization was achieved at different pH and temperatures with the mutated strain Neocallimastix patriciarum. In the study, it was reported that it provides the highest activity at pH=6 and temperature at 62 o C [29].…”

Section: Findings Of Xylanase Enzyme Activity At Different Temperaturesmentioning

confidence: 99%

Determination of In-vitro Optimum Conditions of Xylanase Enzyme Activity Produced by Orpinomyces sp. and Neocallimastix sp.

YÜCEL

Koçer²

2022

JPRI

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This study was aimed to determine the in-vitro optimum conditions of xylanase enzyme activity produced by Orpinomyces sp. and Neocallimastix sp. In the study, xylanase enzyme activity was investigated in terms of extracellular and intracellular total activity (TA) and specific activity (SA) levels at different time (day), pH and temperature levels. Orpinomyces sp. and Neocallimastix sp. when different days (time) were considered in terms of xylanase enzyme activity of fungi species, it was determined that there was a statistically significant positive correlation between TA=0.732 and SA=0.546 (p<0.01). It was determined that there was a statistically positive and significant relationship between TA=0.622 and SA= 0.520 at different pH levels. This situation differs in terms of temperature levels. It was determined that there was a statistically negative significant relationship between genders and SA=-0.354 (p<0.05). In this study, it is thought to contribute by determining the optimum conditions in in-vitro and industrial uses.

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Section: Findings Of Xylanase Enzyme Activity At Different Temperaturesmentioning

confidence: 99%

Determination of In-vitro Optimum Conditions of Xylanase Enzyme Activity Produced by Orpinomyces sp. and Neocallimastix sp.

YÜCEL

Koçer²

2022

JPRI

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“…Chen et al (2012) determined that the optimum pH range of β-glucosidase, which is defined with the number EC3.2.1.21 related to the CAZy enzyme family in the literature, is in the range of 5-6 and its molecular weight is 85.1 kDa. Mountfort et al (1989) reported that the optimum pH for its activity is 5 and the optimum temperature is 55 o C for the xylanase enzyme (EC 3.2.1.8), a member of the GH family.After the commercial use of the xylanase enzyme (Hemi-Cellulase) became widespread, Huang et al (2021) conducted immobilization studies on the gene region related to the xylanase enzyme belonging to Neocallimastix sp. Zhang et al (2019) reported the optimum in vitro working conditions of acetyl xylan esterase (CE -EC3.1.1.72) enzyme, a member of the CAZy enzyme family (Figure 3), which hydrolyzes the ester bonds of acetyl groups in the xylose parts of naturally acidified xylan substrates.…”

Section: Carbohydrate Active Enzymes System In Neocallimastix Spmentioning

confidence: 99%

Carbohydrate active enzyme system in rumen fungi: a review

YÜCEL

EKİNCİ

2022

International Journal of Secondary Metabolite

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Hydrolysis and dehydration reactions of carbohydrates, which are used as energy raw materials by all living things in nature, are controlled by Carbohydrate Active Enzyme (CAZy) systems. These enzymes are also used in different industrial areas today. There are different types of microorganisms that have the CAZy system and are used in the industrial sector. Apart from current organisms, there are also rumen fungi within the group of candidate microorganisms with the CAZy system. It has been reported that xylanase (EC3.2.1.8 and EC3.2.1.37) enzyme, a member of the glycoside hydrolase enzyme family obtained from Trichoderma sp. and used especially in areas such as bread, paper, and feed industry, is more synthesized in rumen fungi such as Orpinomyces sp. and Neocallimastix sp. Therefore, this study reviews Neocallimastixsp., Orpinomyces sp., Caecomyces sp., Piromyces sp., and Anaeromyces sp., registered in the CAZy and Mycocosm database for rumen fungi to have both CAZy enzyme activity and to be an alternative microorganism in the industry. Furthermore the CAZy enzyme activities of the strains are investigated. The review shows thatNeocallimax sp. and Orpinomyces sp. areconsidered as candidate microorganisms.

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“…In the present study, Xylanase was expressed and purified by Escherichia coli from a previous report ( Huang et al, 2021 ), and it was used to enzymatically hydrolyze the wheat bran to prepare feruloyl oligosaccharides. The effect of metal ions on the preparation of feruloyl oligosaccharides through hydrolyzing wheat bran by Xylanase was studied.…”

Section: Introductionmentioning

confidence: 99%

Analysis of the effect of metal ions on the ability of Xylanase to hydrolyze wheat bran by molecular dynamics simulations

Hou

Liang²,

Fei³

et al. 2023

Front. Bioeng. Biotechnol.

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Introduction: Wheat bran is the main by-product of wheat processing, containing about 30% pentosan and 0.4%–0.7% ferulic acid. Wheat bran is the main raw material used to prepare feruloyl oligosaccharides by hydrolysis of Xylanase, we discovered that the ability of Xylanase to hydrolyze wheat bran could be affected in the presence of different metal ions.Methods: In the present study, we have probed the effects of different metal ions on the hydrolysis activity of Xylanase on wheat bran and tried to analyze the effect of Mn2+ and Xylanase by molecular dynamic (MD) simulation.Results: Our results suggested that Mn2+ had improved the Xylanase hydrolyzing wheat bran to obtain feruloyl oligosaccharides. Particularly when the concentration of Mn2+ reached 4 mmol/L, the optimal product has been obtained 2.8 times higher to compare with no addition. Through the MD simulation analysis, our results reveal that Mn2+ can induce structural change in the active site, which enlarges the substrate binding pocket. The simulation results also revealed that the addition of Mn2+ resulted in a low RMSD value compared with the absence of Mn2+ and helped stabilize the complex.Conclusion: Mn2+ could increase the enzymatic activity of Xylanase in the hydrolysis of feruloyl oligosaccharides in wheat bran. The finding could have significant implications for the preparation of feruloyl oligosaccharides from wheat bran.

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Immobilization of mutated xylanase from Neocallimastix patriciarum in E. coli and application for kraft pulp biobleaching

Cited by 5 publications

References 35 publications

Determination of In-vitro Optimum Conditions of Xylanase Enzyme Activity Produced by Orpinomyces sp. and Neocallimastix sp.

Determination of In-vitro Optimum Conditions of Xylanase Enzyme Activity Produced by Orpinomyces sp. and Neocallimastix sp.

Carbohydrate active enzyme system in rumen fungi: a review

Analysis of the effect of metal ions on the ability of Xylanase to hydrolyze wheat bran by molecular dynamics simulations

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