Catalytic properties of the immobilized Talaromyces thermophilus β-xylosidase and its use for xylose and xylooligosaccharides production

Guerfali, Mohamed; Maalej, Ines; Gargouri, Ali; Belghith, Hafedh

doi:10.1016/j.molcatb.2008.09.011

Cited by 37 publications

(16 citation statements)

References 38 publications

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“…Schofield, Patchett, and Parker (2004) also mentioned that enzyme activity is restored by a wide range of divalent metal ions including (in order of decreasing effectiveness): Zn 2+ , Cd 2+ , Mn 2+ , Co 2+ , Ni 2+ , Ca 2+ , Hg 2+ , and Cu 2+ (Schofield, Patchett, & Parker, 2004). Native and immobilized β-xylosidases were found to be stimulated by Ca 2+ , Mn 2+ , and Co 2+ (Guerfali, Maalej, Gargouri, & Belghith, 2009). Fazary pointed that activity of Aspergillus awamori feruloyl esterase can be activated by Ca 2+ (Fazary, Ismadji, & Ju, 2009).…”

Section: Introductionmentioning

confidence: 98%

Degumming of ramie bast fibers by Ca²⁺-activated composite enzyme

Qiang

Yan

2013

Journal of The Textile Institute

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In recent years, special attention has been paid to the application of biotechnology in the textile industry. In this study, composite enzyme (contained pectatelyase/hemicellulase/laccase) was employed to degum the ramie bast successfully. Interestingly, the activities of enzymes were enhanced by promotion of Ca 2+ activated remarkably. The test of degummed ramie fiber performance demonstrated that fiber fineness, breaking strength, whiteness, and residual gum of fibers have greatly improved. Further, the structure and morphous of the fibers before and after degumming was examined and analyzed. The results showed that the gum, hemicellulose, and lignin were removed effectively and treated fibers had the typical cellulose I structure suitable for direct textile and other applications. These outcomes suggested that Ca 2+ -activated composite enzyme could degum the gum of ramie bast effectively, which provided a method to improve the quality of ramie fibers and a theoretical basis for flax degumming technique on an environmentally-friendly basis.

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Section: Introductionmentioning

confidence: 98%

Degumming of ramie bast fibers by Ca²⁺-activated composite enzyme

Qiang

Yan

2013

Journal of The Textile Institute

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“…Many xylanolytic enzymes have been individually immobilized by different methods; and some studies have investigated the co-immobilization of two xylanolytic enzymes [8]. In this sense, the xylanase and β-xylosidase from Talaromyces thermophilus were co-immobilized on chitosan and employed for the hydrolysis of oat spelt xylan, demonstrating the synergistic action of both enzymes by increasing the saccharification of the substrate [9]. In another study, co-immobilization of recombinant xylanase and α-L-arabinofuranosidase in glyoxyl agarose was evaluated through different approaches in the hydrolysis of xylan for the production of non-arabinosylated xylan [10].…”

Section: Introductionmentioning

confidence: 99%

Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis

Terrasan

Trobo-Maseda

Moreno-Pérez

et al. 2016

Process Biochemistry

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Differently activated agarose-based supports were evaluated for co-immobilization of a crude extract from Penicillium janczewskii containing xylanase, β-xylosidase and α-Larabinofuranosidase activities. Adequately selecting support and immobilization conditions (8 h, using agarose with 10% crosslinking) increased enzyme levels substantially, mainly in relation to the xylanase (2-fold). A coating with dextran aldehyde MW 6,000 Da, partially oxidized, covalently attached the enzymes to the support. Optimum activity was verified in the pH range 2-4, and at 50, 65 and 80 °C for the xylanase, α-L-arabinofuranosidase and β-xylosidase, 2 respectively. The xylanase was highly thermostable retaining more than 70% of activity even after 24 h incubation at 60 and 70 °C; and at 80 °C its half-life was 1.7 h. The half-lives of the β-xylosidase and α-L-arabinofuranosidase at 50 °C were 2.3 and 3.8 h, respectively. The coimmobilization of the enzymes on a single support give raise to a functional multi-enzymatic biocatalyst acting in the complete hydrolysis of different and complex substrates such as oat spelt and wheat arabinoxylans, with xylose yield higher than 40%. The xylanase and the α-Larabinofuranosidase presented high stability retaining 86.6 and 88.0% of activity after 10 reuse cycles.

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“…Xylanases can improve the hydrolysis of cellulose into fermentable sugars by depolymerizing xylans from the cellulose-hemicellulose compound, and furthermore enhance the access of cellulases to cellulose surfaces [8,9]. β-Xylosidases, displaying the similar function as xylanases, are important part of most microbial xylanolytic systems by attacking the non-reducing ends of XOs to release xylose or other oligosaccharides [10-13]. The catalytic process of β-xylosidases is considered as a double displacement mechanism requiring a glycosyl enzyme medium, like the catalysis of glycosidases [10].…”

Section: Introductionmentioning

confidence: 99%

Biochemical properties of a novel thermostable and highly xylose-tolerant β-xylosidase/α-arabinosidase from Thermotoga thermarum

Shi¹,

Li²,

Gu³

et al. 2013

Biotechnol Biofuels

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Backgroundβ-Xylosidase is an important constituent of the hemicellulase system and it plays an important role in hydrolyzing xylooligosaccharides to xylose. Xylose, a useful monose, has been utilized in a wide range of applications such as food, light, chemical as well as energy industry. Therefore, the xylose-tolerant β-xylosidase with high specific activity for bioconversion of xylooligosaccharides has a great potential in the fields as above.ResultsA β-xylosidase gene (Tth xynB3) of 2,322 bp was cloned from the extremely thermophilic bacterium Thermotoga thermarum DSM 5069 that encodes a protein containing 774 amino acid residues, and was expressed in Escherichia coli BL21 (DE3). The phylogenetic trees of β-xylosidases were constructed using Neighbor-Joining (NJ) and Maximum-Parsimony (MP) methods. The phylogeny and amino acid analysis indicated that the Tth xynB3 β-xylosidase was a novel β-xylosidase of GH3. The optimal activity of the Tth xynB3 β-xylosidase was obtained at pH 6.0 and 95°C and was stable over a pH range of 5.0-7.5 and exhibited 2 h half-life at 85°C. The kinetic parameters Km and Vmax values for p-nitrophenyl-β-D-xylopyranoside and p-nitrophenyl-α-L-arabinofuranoside were 0.27 mM and 223.3 U/mg, 0.21 mM and 75 U/mg, respectively. The kcat/Km values for p-nitrophenyl-β-D-xylopyranoside and p-nitrophenyl-α-L-arabinofuranoside were 1,173.4 mM-1 s-1 and 505.9 mM-1 s-1, respectively. It displayed high tolerance to xylose, with Ki value approximately 1000 mM. It was stimulated by xylose at higher concentration up to 500 mM, above which the enzyme activity of Tth xynB3 β-xylosidase was gradually decreased. However, it still remained approximately 50% of its original activity even if the concentration of xylose was as high as 1000 mM. It was also discovered that the Tth xynB3 β-xylosidase exhibited a high hydrolytic activity on xylooligosaccharides. When 5% substrate was incubated with 0.3 U Tth xynB3 β-xylosidase in 200 μL reaction system for 3 h, almost all the substrate was biodegraded into xylose.ConclusionsThe article provides a useful and novel β-xylosidase displaying extraordinary and desirable properties: high xylose tolerance and catalytic activity at temperatures above 75°C, thermally stable and excellent hydrolytic activity on xylooligosaccharides.

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Catalytic properties of the immobilized Talaromyces thermophilus β-xylosidase and its use for xylose and xylooligosaccharides production

Cited by 37 publications

References 38 publications

Degumming of ramie bast fibers by Ca²⁺-activated composite enzyme

Degumming of ramie bast fibers by Ca²⁺-activated composite enzyme

Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis

Biochemical properties of a novel thermostable and highly xylose-tolerant β-xylosidase/α-arabinosidase from Thermotoga thermarum

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Catalytic properties of the immobilized Talaromyces thermophilus β-xylosidase and its use for xylose and xylooligosaccharides production

Cited by 37 publications

References 38 publications

Degumming of ramie bast fibers by Ca2+-activated composite enzyme

Degumming of ramie bast fibers by Ca2+-activated composite enzyme

Co-immobilization and stabilization of xylanase, β-xylosidase and α-l-arabinofuranosidase from Penicillium janczewskii for arabinoxylan hydrolysis

Biochemical properties of a novel thermostable and highly xylose-tolerant β-xylosidase/α-arabinosidase from Thermotoga thermarum

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Degumming of ramie bast fibers by Ca²⁺-activated composite enzyme

Degumming of ramie bast fibers by Ca²⁺-activated composite enzyme