Origins and features of pectate lyases and their applications in industry

Wu, Pan; Yang, Shihui; Zhan, Zongxiang; Zhang, Guimin

doi:10.1007/s00253-020-10769-8

Cited by 30 publications

(20 citation statements)

References 108 publications

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“…However, its optimum temperature is in the range of that measured for X. campestris Pel [73] and cold-active Pel1 from M. eurypsychrophila [74]. The lack of disulphide bridges previously shown in the structure could be responsible for the lower stability of the enzyme at high temperatures, in comparison with previously characterized PLs [75].…”

Section: Resultsmentioning

confidence: 88%

The structural, dynamical and biochemical characterizations ofVerticillium dahliaepectate lyase, VdPelB, highlight its specificities

Safran

Ung

Bouckaert

et al. 2022

Preprint

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Pectins, complex polysaccharides and major components of the plant primary cell wall, can be degraded by pectate lyases (PLs). PLs cleave glycosidic bonds of homogalacturonans (HG), the main pectic domain, by beta-elimination, releasing unsaturated oligogalacturonides (OGs). To understand the catalytic mechanism and structure/function of these enzymes, we characterized VdPelB from Verticillium dahliae, a plant pathogen. We first solved the crystal structure of VdPelB at 1.2A resolution showing that it is a right-handed parallel beta-helix structure. Molecular dynamics (MD) simulations further highlighted the dynamics of the enzyme in complex with substrates that vary in their degree of methylesterification, identifying amino acids involved in substrate binding and cleavage of non-methylesterified pectins. We then biochemically characterized wild type and mutated forms of VdPelB. VdPelB was most active on non-methylesterified pectins, at pH 8 in presence of Ca2+ ions. VdPelB-G125R mutant was most active at pH 9 and showed higher relative activity compared to native enzyme. The OGs released by VdPelB differed to that of previously characterized PLs, showing its peculiar specificity in relation to its structure. OGs released from Verticillium-partially tolerant and sensitive flax cultivars differed which could facilitate the identification VdPelB-mediated elicitors of defence responses.

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Section: Resultsmentioning

confidence: 88%

The structural, dynamical and biochemical characterizations ofVerticillium dahliaepectate lyase, VdPelB, highlight its specificities

Safran

Ung

Bouckaert

et al. 2022

Preprint

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“…Correlation equations ( 11) and ( 12) reflect the interrelation between the parameters in the low-modulus modification regime El warp ¼ EI LF warp À 0:009 Á N 30 þ 0:88 Á A À 0:0013 Á AN 30 ; r ¼ 0:9915 (11) El weft ¼ EI LF weft À 0:0071 Á N 30 þ 0:923 Á A À 0:0015 Á AN 30 ; ¼ 0:9909 (12) An analysis of Equations ( 11) and (12) indicates that the higher content of small-sized cellulases in the preparations and their effect on the flax fiber cell wall G-layer facilitate stiffness reduction. However, the role of the first variable term in the equations is extremely low.…”

Section: Stiffness Testmentioning

confidence: 99%

“…[7][8][9] A great deal of attention has been paid by researchers to enzymatic methods of fabric production from bast-fiber plants. [10][11][12] A common question is the choice of biocatalyst used for ramie degumming in one of the recommended processing methods based on pectinases, pectate lyases or xylanases and their compositions. [13][14][15][16][17] Fiber biomodification has made it possible to increase the mechanical strength, fiber spinnability and capillarity, and also to decrease yellowness after bleaching and to provide fabrics with higher dyeing quality in comparison with that achieved by chemical treatment.…”

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confidence: 99%

Justification of an approach to cellulase application in enzymatic softening of linen fabrics and clothing

Кокшаров

Bikbulatova

Корнилова

et al. 2022

Textile Research Journal

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We propose the final softening finishing of textile products based on a complex of modifying effects on a highly ordered cellulose backbone of the secondary cell wall G-layer or on a mesh corset of microfibrillar cellulose in the primary cell wall. We suggest using polypeptide molecule sizes and the strength of polypeptide molecule adsorption binding on a model solid-phase substrate as parameters of the structurally regulated action of cellulase preparations. The article presents an analysis of 11 cellulase preparations as groups of weakly, tightly and medium adsorption enzymes, and also groups of volumetric, peripheral or combined activity manifested in the fiber structure. We show the regularities of enzyme property influence on the fiber pore structure development, changes in the parameters of the fabric bending stiffness and breaking load and technological shrinkage for two modification modes: liquid treatment with flax fiber swelling or low-modulus application solution. For the liquid method of treatment (with a bath module of at least 10) it is recommended to apply highly adsorbable cellulases ( A > 50%), in which the content of molecules with a globule size less than 30 nm does not exceed 15%. For the low-modulus method of treatment it is recommended to use enzymes with the adsorption capacity of at least 40% and a low content of small-sized fractions (no more than 25%). The recommended treatment variants ensure a three to four-fold bending stiffness decrease at the mechanical strength loss of not more than 15% and shrinkage of linen fabrics not more than 0.5%.

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“…pectate lyases). 188,189 Other applications include alginate degradation, 190 bioengineering/synthetic biology assays and the synthesis of aromatic compounds, plastics, cosmetics and adhesive precursors. 191 As with other enzyme classes, lyases can be used in free and immobilized forms.…”

Section: Lyasesmentioning

confidence: 99%

Enzyme immobilization: what have we learned in the past five years?

Almeida

Prata

Forte

2021

Biofuels Bioprod Bioref

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Immobilized enzymes have been widely applied in several fields over the past years, and the number of studies on the topic has been rapidly increasing. This review aimed to examine changes and trends in enzyme immobilization research during the past five years. Data were collected from the Web of Science Core Collection database and analyzed using VOSviewer © software. A discussion is presented on the most productive countries, most cited authors, leading publications, main areas of research and industrial applications of immobilized enzymes. China, the USA, India, Brazil and Spain hold the largest numbers of published articles on the topic, and the two main areas of study are chemistry and biotechnology applied microbiology. Trend analysis showed that laccases and lipases were the most commonly used enzymes, whereas nanoparticles and metal-organic frameworks were the most commonly used enzyme supports. The results highlight that immobilization is used to modify several enzyme properties, such as stability, recovery and specificity. Conclusions and future perspectives in the field are also addressed. It is believed that the development of new, low-cost supports and studies on the scale-up of processes using immobilized enzymes constitute future research trends.

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Origins and features of pectate lyases and their applications in industry

Cited by 30 publications

References 108 publications

The structural, dynamical and biochemical characterizations ofVerticillium dahliaepectate lyase, VdPelB, highlight its specificities

The structural, dynamical and biochemical characterizations ofVerticillium dahliaepectate lyase, VdPelB, highlight its specificities

Justification of an approach to cellulase application in enzymatic softening of linen fabrics and clothing

Enzyme immobilization: what have we learned in the past five years?

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