The β-xylosidase from Ceratocystis fimbriata RM35 improves the saccharification of sugarcane bagasse

Martins, Marcele Pandeló; Ventorim, Rafaela Zandonade; Coura, Roberta Ribeiro; Maitan-Alfenas, Gabriela Píccolo; Alfenas, Rafael Ferreira; Guimarães, Valéria Monteze

doi:10.1016/j.bcab.2018.01.009

Cited by 14 publications

(11 citation statements)

References 43 publications

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“…Second, α-arabinofuranosidase, acetylesterase, α-glucuronidase and ferulic acid esterase cleave the side-chain substituents [ 8 ]. In the last step, β-xylosidase, which is well known as the major hydrolytic enzyme that degrades the non-reducing ends of β-1,4-linked D-xylose residues to release xylose as the final product from short xylooligosaccharides [ 9 , 10 ]. However, the roles of β-xylosidase include, but are not limited to, the degradation of xylooligosaccharide.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a novel thermostable and xylose-tolerant GH 39 β-xylosidase from Dictyoglomus thermophilum

et al. 2018

BMC Biotechnol

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Backgroundβ-D-xylosidase is a vital exoglycosidase with the ability to hydrolyze xylooligosaccharides to xylose and to biotransform some saponins by cleaving outer β-xylose. β-D-xylosidase is widely used as one of the xylanolytic enzymes in a diverse range of applications, such as fuel, food and the pharmaceutical industry; therefore, more and more studies have focused on the thermostable and xylose-tolerant β-D-xylosidases.ResultsA thermostable β-xylosidase gene (xln-DT) of 1509 bp was cloned from Dictyoglomus thermophilum and expressed in E.coli BL21. According to the amino acid and phylogeny analyses, the β-xylosidase Xln-DT is a novel β-xylosidase of the GH family 39. The recombinant β-xylosidase was purified, showing unique bands on SDS-PAGE, and had a protein molecular weight of 58.7 kDa. The β-xylosidase Xln-DT showed an optimal activity at pH 6.0 and 75 °C, with p-nitrophenyl-β-D-xylopyranoside (pNPX) as a substrate. Xln-DT displayed stability over a pH range of 4.0-7.5 for 24 h and displayed thermotolerance below 85 °C. The values of the kinetic parameters Km and Vmax for pNPX were 1.66 mM and 78.46 U/mg, respectively. In particular, Xln-DT displayed high tolerance to xylose, with 60% activity in the presence of 3 M xylose. Xln-DT showed significant effects on the hydrolyzation of xylobiose. After 3 h, all the xylobiose tested was degraded into xylose. Moreover, β-xylosidase Xln-DT had a high selectivity for cleaving the outer xylose moieties of natural saponins, such as notoginsenoside R1 and astragaloside IV, which produced the ginsenoside Rg1 with stronger anti-fatigue activity and produced cycloastragenol with stronger anti-aging activity, respectively.ConclusionThis study provides a novel GH 39 β-xylosidase displaying extraordinary properties of highly catalytic activity at temperatures above 75 °C, remarkable hydrolyzing activity of xylooligosaccharides and rare saponins producing ability in the pharmaceutical and commercial industries.Electronic supplementary materialThe online version of this article (10.1186/s12896-018-0440-3) contains supplementary material, which is available to authorized users.

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Section: Introductionmentioning

confidence: 99%

Characterization of a novel thermostable and xylose-tolerant GH 39 β-xylosidase from Dictyoglomus thermophilum

et al. 2018

BMC Biotechnol

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“…However, some studies are comparable with ours, such as those using Lichtheimia ramose by Garcia et al (2015) which have shown a maximal β-xylosidase activity (11.57 U.mL -1 ) in the presence of wheat bran, after 4 days fermentation. Ceratocystis fimbriata RM 35 when grown on wheat bran for 7 days was also able to produce 14.40 U.mL -1 of β-xylosidase (Martins et al, 2018). Even though, our results were obtained after 48 hrs, which can be considered a great advantage.…”

Section: Determination Of Physico-chemical Properties Of Enzymesmentioning

confidence: 52%

“…Concerning BXU, it is common to observed in literature an acidophilic and thermophilic profile, with optima of pH and temperature around 4.0-5.0, and between 65-70°C, as observed for Aspergillus (Díaz-Malváez et al, 2013;Wakiyama et al, 2008) and Ceratocystis strains (Martins et al, 2018). Terrasan et al (2011) observed the best condition for β-xylosidase when the enzymatic extract was incubated at 75°C and pH 5.0 from P. janczewskii.…”

Section: Determination Of Physico-chemical Properties Of Enzymesmentioning

confidence: 92%

“…thermophila M.7.7, but a different result was observed for Ba 2+ and Mg 2+ , where no inhibition was detected. Some studies have reported the apparent activation of fungal BXU by Mn 2+ and Ca 2+ , suggesting that these ions activate and protect the active site (Yang et al, 2014;Pereira et al, 2015;Martins et al, 2018). Terrasan et al (2011) observed a slight inhibition of β-xylosidase from P. janczewskii by Mn 2+ (17%) and Ca 2+ (21%), whereas Bonfa et al 2018, have shown an inhibition of 50% by Mn 2+ for the β-xylosidase from crude extract from M. thermophila M.7.7.…”

Section: Determination Of Physico-chemical Properties Of Enzymesmentioning

confidence: 99%

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Trichoderma atroviride 102C1: A promising mutant strain for the production of a -glucosidase, -xylosidase and -L-arabinofuranosidase activities using agroindustrial by-products

Silva¹,

Grigorevski-Lima²,

Bon³

et al. 2018

Afr. J. Biotechnol.

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Holocellulolytic accessory enzymes are very important in assisting hydrolysis of biomass. The use of these enzymes in the enzymatic hydrolysis of plant biomass is very important for obtaining building blocks in the concept of biorefinery. In previous studies, the mutant strain Trichoderma atroviride 102C1 was tested for production of endoglucanases, FPases and endoxylanases. This study aimed at evaluating the efficiency in holocellulolytic accessories enzymes production (-glucosidase, xylosidase and -L-arabinofuranosidase) by Trichoderma atroviride 102C1 using different lignocelluloses biomass as substrates. Accessory enzymes production was carried out in Erlenmeyer flasks containing Mandels salt medium, supplemented with different concentrations of sugarcane bagasse (SCB) and corn steep liquor (CSL), according to a Central Composite Rotational Design (CCRD). The fermentation system was incubated under agitation for 2 days / 28°C. For pH and temperature profile studies, a new CCRD was carried out. The best condition common to all enzymes, 55.4 U.mL-1 (β-glucosidase), 10.8 U.mL-1 (β-xylosidase) and 143.23 U.mL-1 (α-L-arabinofuranosidase), was observed when 2.5% (w/v) sugarcane bagasse (SCB) and 1.26% (w/v) of corn steep liquor (CSL) were used. All enzymes presented acidophilic characteristic in two different temperatures (44 and 55°C). The optimal profile characteristic for β-glucosidase and β-xylosidase activities were pH 5.0 and 3.0, respectively, both at 55°C, while for α-L-arabinofuranosidase it was pH 3.6 at 44°C. This study demonstrated the potential of T. atroviride 102C1 to produce three important holocellulolytic accessory enzymes in the presence of SCB and CSL, suggesting its use for enzymatic hydrolysis of lignocellulosic biomass.

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“…Ceratocystis fimbriata was firstly described by Halsted in 1980, causing sweet potato rot, and it is largely found in several environments, mainly attacking crops in tropical climate areas [15]. This fungus is able to produce an accessory enzyme, β-xylosidase, essential for hemicellulose hydrolysis of sugarcane bagasse [16]. Fusarium verticillioides cause disease on maize plantations representing a serious economic threat to its production and quality [17].…”

Section: Enzymes From Phytopathogenic Fungimentioning

confidence: 99%

Phytopathogenic Fungi: Useful Tools to Degrade Plant Biomass for Bioethanol Production

Maitan-Alfenas¹

2019

MCDA

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Phytopathogenic fungi are able to produce enzymes for cell wall degradation when they attack the hosts and there is a close relationship between the capacity of enzymatic secretion and the virulence of these microorganisms. These enzymes are promising for biotechnological purposes and plant biomasses play an important role for induction of their production by fungal species. Biomass is an economic alternative to reduce pollution and to produce renewable fuels. The fungal enzymes are mainly applied for the hydrolysis step of bioethanol production process, which is environmentally friend. Many phytopathogen fungi are considered promising for enzymes production such as Chrysoporthe cubensis, Ceratocystis fimbriata and Fusarium verticillioides.

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The β-xylosidase from Ceratocystis fimbriata RM35 improves the saccharification of sugarcane bagasse

Cited by 14 publications

References 43 publications

Characterization of a novel thermostable and xylose-tolerant GH 39 β-xylosidase from Dictyoglomus thermophilum

Characterization of a novel thermostable and xylose-tolerant GH 39 β-xylosidase from Dictyoglomus thermophilum

Trichoderma atroviride 102C1: A promising mutant strain for the production of a -glucosidase, -xylosidase and -L-arabinofuranosidase activities using agroindustrial by-products

Phytopathogenic Fungi: Useful Tools to Degrade Plant Biomass for Bioethanol Production

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