Rhizobium spp exopolysaccharides production and xanthan lyase use on its structural modification

Sousa, Bruna Fernanda Silva de; Castellane, Tereza Cristina Luque; Campanharo, João Carlos; Lemos, Eliana Gertrudes de Macedo

doi:10.1016/j.ijbiomac.2019.06.077

Cited by 9 publications

(4 citation statements)

References 57 publications

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“…Rhizobium EPS are used as stabilizers of fungal laccase or to counteract drought and prevent soil erosion. Improving the properties of the EPS after treatment with xanthan lyase expands the scope of possible applications of this polysaccharide (de Sousa et al 2019 ).…”

Section: Prospects For the Application Of Xanthan-active Enzymesmentioning

confidence: 99%

Xanthan: enzymatic degradation and novel perspectives of applications

Berezina,

Rykov,

Schwarz

et al. 2024

Appl Microbiol Biotechnol

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The extracellular heteropolysaccharide xanthan, synthesized by bacteria of the genus Xanthomonas, is widely used as a thickening and stabilizing agent across the food, cosmetic, and pharmaceutical sectors. Expanding the scope of its application, current efforts target the use of xanthan to develop innovative functional materials and products, such as edible films, eco-friendly oil surfactants, and biocompatible composites for tissue engineering. Xanthan-derived oligosaccharides are useful as nutritional supplements and plant defense elicitors. Development and processing of such new functional materials and products often necessitate tuning of xanthan properties through targeted structural modification. This task can be effectively carried out with the help of xanthan-specific enzymes. However, the complex molecular structure and intricate conformational behavior of xanthan create problems with its enzymatic hydrolysis or modification. This review summarizes and analyzes data concerning xanthan-degrading enzymes originating from microorganisms and microbial consortia, with a particular focus on the dependence of enzymatic activity on the structure and conformation of xanthan. Through a comparative study of xanthan-degrading pathways found within various bacterial classes, different microbial enzyme systems for xanthan utilization have been identified. The characterization of these new enzymes opens new perspectives for modifying xanthan structure and developing innovative xanthan-based applications. Key points • The structure and conformation of xanthan affect enzymatic degradation. • Microorganisms use diverse multienzyme systems for xanthan degradation. • Xanthan-specific enzymes can be used to develop xanthan variants for novel applications.

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Section: Prospects For the Application Of Xanthan-active Enzymesmentioning

confidence: 99%

Xanthan: enzymatic degradation and novel perspectives of applications

Berezina,

Rykov,

Schwarz

et al. 2024

Appl Microbiol Biotechnol

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“…In contrast, xanthan in its disordered conformation demonstrated gel-like behavior with no chain relaxation [9]. Solubility [11], rheology[12], stability [13], and other properties are easily changed by affecting chemical methods such as copolymerization[14,15],using chemical substances such as acids and surfactants for treatment [11,15,16], and biological methods as fermentation [17,18,19].All these methods can be used to modify xanthan gum. The current work concentrates on the rheological properties of xanthan grafted with styrene.Styrene (phenylethylene) is a key petrochemical product used to make polymers (polystyrene, synthetic rubber) and copolymers (high-impact polystyrene).…”

Section: Introductionmentioning

confidence: 99%

Modification of Xanthan Gum with Styrene and Investigation of its Rheological Properties

Kusherova,

Negim,

Aidarova

et al. 2023

Egypt. J. Chem.

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A "green" polymer made by bacteria, xanthan gum has several applications in both the food and drug industries. Because of its harmlessness, xanthan gum is frequently used in other fields after quality improvement through modification. This article describes the grafting process of xanthan gum with styrene and investigates the rheological properties of the modified (grafted) copolymer. For copolymerization, different ratios of xanthan and styrene compositions (XG: St -1:1.6, 1:5, and 1:8 w/w%) were used. The FTIR spectra of XG-g-St revealed an increase at 1120 cm -1 , indicating the formation of additional ether groups due to the St and XG interaction. The rheology properties were investigated at 30, 60, and 80°C. The shear stress of XG dropped from 30 to 80°C, with a maximum shear stress value of 8 Pa at 30°C and a minimum value of 5 Pa at 80°C.According to the findings, grafted with styrene xanthan gum has higher shear stress and better resistance to temperature in comparison with un-modified pure xanthan gum. Due to the grafting new side chains and bonds appear on polymer molecules which affect its viscoelasticity. These findings could be useful in a variety of fields, including oil recovery and construction.

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“…Previous reports demonstrated that modifications of side chain have great impacts on xanthan’s rheological properties, solubility and dispersion (Riaz et al 2021 ). Notably, xanthan with truncated side chain is less susceptible to high temperature (De Sousa et al 2019 ). Some Xanthomonas campestris strains have been genetically engineered to produce xanthan with modified side chains, but the yield of which cannot meet the industrial demands (Tait et al 1989 ).…”

Section: Introductionmentioning

confidence: 99%

Dissecting the essential role of N-glycosylation in catalytic performance of xanthan lyase

Zhao

Wang

et al. 2022

Bioresour. Bioprocess.

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Modified xanthan produced by xanthan lyase has broad application prospects in the food industry. However, the catalytic performance of xanthan lyase still needs to be improved through rational design. To address this problem, in this work, the glycosylation and its influences on the catalytic performance of a xanthan lyase (EcXly), which was heterologously expressed in Escherichia coli, were reported. Liquid chromatography coupled to tandem mass spectrometry analysis revealed that the N599 site of EcXly was modified by a single N-glycan chain. Based on sequence alignment and three-dimensional structure prediction, it could be deduced that the N599 site was located in the catalytic domain of EcXly and in close proximity to the catalytic residues. After site-directed mutagenesis of N599 with alanine, aspartic acid and glycine, respectively, the EcXly and its mutants were characterized and compared. The results demonstrated that elimination of the N-glycosylation had diminished the specific activity, pH stability, and substrate affinity of EcXly. Fluorescence spectra further revealed that the glycosylation could significantly affect the overall tertiary structure of EcXly. Therefore, in prokaryotic hosts, the N-glycosylation could influence the catalytic performance of the enzyme by changing its structure. To the best of our knowledge, this is the first report about the post-translational modification of xanthan lyase in prokaryotes. Overall, our work enriched research on the role of glycan chains in the functional performance of proteins expressed in prokaryotes and should be valuable for the rational design of xanthan lyase to produce modified xanthan for industrial application. Graphical Abstract

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Rhizobium spp exopolysaccharides production and xanthan lyase use on its structural modification

Cited by 9 publications

References 57 publications

Xanthan: enzymatic degradation and novel perspectives of applications

Xanthan: enzymatic degradation and novel perspectives of applications

Modification of Xanthan Gum with Styrene and Investigation of its Rheological Properties

Dissecting the essential role of N-glycosylation in catalytic performance of xanthan lyase

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