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

Terrasan, César Rafael Fanchini; Trobo-Maseda, Lara; Moreno-Pérez, Sonia; Carmona, Eleonora Cano; Pessela, Benevides C.; Guisán, José M.

doi:10.1016/j.procbio.2016.02.014

Cited by 17 publications

(8 citation statements)

References 38 publications

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“…Besides dextransucrase encapsulation, the co-immobilization of this enzyme with dextranase (EC 3.2.1.11) is another way to efficiently synthesize dextrans and oligosaccharides [238,273]. This technology allows the design of novel multi-functional biocatalysts and can display benefits owing to the synergy of the enzymes [274,275]. However, the challenge of this kind of co-immobilization is to avoid the inactivation of dextransucrase that is promoted by dextranase.…”

Section: The Gh 70 Family Of Enzymesmentioning

confidence: 99%

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

et al. 2016

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Glycoside hydrolases (GH) are enzymes capable to hydrolyze the glycosidic bond between two carbohydrates or even between a carbohydrate and a non-carbohydrate moiety. Because of the increasing interest for industrial applications of these enzymes, the immobilization of GH has become an important development in order to improve its activity, stability, as well as the possibility of its reuse in batch reactions and in continuous processes. In this review, we focus on the broad aspects of immobilization of enzymes from the specific GH families. A brief introduction on methods of enzyme immobilization is presented, discussing some advantages and drawbacks of this technology. We then review the state of the art of enzyme immobilization of families GH1, GH13, and GH70, with special attention on the enzymes β-glucosidase, α-amylase, cyclodextrin glycosyltransferase, and dextransucrase. In each case, the immobilization protocols are evaluated considering their positive and negative aspects. Finally, the perspectives on new immobilization methods are briefly presented.

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Section: The Gh 70 Family Of Enzymesmentioning

confidence: 99%

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

et al. 2016

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“…This derivative was more stable than the glyoxyl derivative of S. ruminantium β-xylosidase, which presented 39% residual activity during eight pNPX hydrolysis cycles [16], that may be attributed to the less BXYL I subunits (two subunits), while S. ruminantium β-xylosidase is tetrameric [39]. Moreover, due to its high operational stability, this derivative can be potentially used to complement the derivative containing the co-immobilized xylanase, β-xylosidase, and α-L-arabinofuranosidase from P. janczewskii, because the β-xylosidase is faintly stable in this biocatalyst [20].…”

Section: Reuse Cyclesmentioning

confidence: 99%

“…In another study, the crude xylanase, β-xylosidase, and α-L-arabinofuranosidase were co-immobilized providing a biocatalyst active in the degradation of different arabinoxylans. In this preparation, the β-xylosidase was poorly stable under operational conditions [20]. In this work, we sought to purify and characterize a second extracellular βxylosidase from P. janczewskii (BXYL II), which is present to a lesser extent in the culture filtrate.…”

Section: Introductionmentioning

confidence: 99%

Immobilization and Stabilization of Beta-Xylosidases from Penicillium janczewskii

Terrasan

Romero‐Fernández

Orrego

et al. 2016

Appl Biochem Biotechnol

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β-Xylosidases are critical for complete degradation of xylan, the second main constituent of plant cell walls. A minor β-xylosidase (BXYL II) from Penicillium janczewskii was purified by ammonium sulfate precipitation (30% saturation) followed by DEAE-Sephadex chromatography in pH 6.5 and elution with KCl. The enzyme presented molecular weight (MW) of 301 kDa estimated by size exclusion chromatography. Optimal activity was observed in pH 3.0 and 70-75 °C, with higher stability in pH 3.0-4.5 and half-lives of 11, 5, and 2 min at 65, 70, and 75 °C, respectively. Inhibition was moderate with Pb and citrate and total with Cu, Hg, and Co. Partially purified BXYL II and BXYL I (the main β-xylosidase from this fungus) were individually immobilized and stabilized in glyoxyl agarose gels. At 65 °C, immobilized BXYL I and BXYL II presented half-lives of 4.9 and 23.1 h, respectively, therefore being 12.3-fold and 33-fold more stable than their unipuntual CNBr derivatives (reference mimicking soluble enzyme behaviors). During long-term incubation in pH 5.0 at 50 °C, BXYL I and BXYL II glyoxyl derivatives preserved 85 and 35% activity after 25 and 7 days, respectively. Immobilized BXYL I retained 70% activity after 10 reuse cycles of p-nitrophenyl-β-D-xylopyranoside hydrolysis.

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“…To date, several strategies have been performed for xylose bioproduction from xylans of different sources on the basis of co-cation of the two types of xylanolytic enzymes [9, 10]. However, the xylose yields still remain low [11]. Hence, identification of novel xylanolytic enzymes suitable for high-efficient production of xylose from xylan is still of great importance.…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterization of a novel exo-oligoxylanase from Paenibacillus barengoltzii suitable for monosaccharification from corncobs

Liu

Jiang

Liu

et al. 2019

Biotechnol Biofuels

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Background Xylan is the major component of hemicelluloses, which are the second most abundant polysaccharides in nature, accounting for approximately one-third of all renewable organic carbon resources on earth. Efficient degradation of xylan is the prerequisite for biofuel production. Enzymatic degradation has been demonstrated to be more attractive due to low energy consumption and environmental friendliness, when compared with chemical degradation. Exo-xylanases, as a rate-limiting factor, play an important role in the xylose production. It is of great value to identify novel exo-xylanases for efficient bioconversion of xylan in biorefinery industry. Results A novel glycoside hydrolase (GH) family 8 reducing-end xylose-releasing exo-oligoxylanase (Rex)-encoding gene ( PbRex8 ) was cloned from Paenibacillus barengoltzii and heterogeneously expressed in Escherichia coli . The deduced amino acid sequence of PbRex8 shared the highest identity of 74% with a Rex from Bacillus halodurans. The recombinant enzyme (PbRex8) was purified and biochemically characterized. The optimal pH and temperature of PbRex8 were 5.5 and 55 °C, respectively. PbRex8 showed prominent activity on xylooligosaccharides (XOSs), and trace activity on xylan. It also exhibited β-1,3-1,4-glucanase and xylobiase activities. The enzyme efficiently converted corncob xylan to xylose coupled with a GH family 10 endo-xylanase, with a xylose yield of 83%. The crystal structure of PbRex8 was resolved at 1.88 Å. Structural comparison suggests that Arg67 can hydrogen-bond to xylose moieties in the -1 subsite, and Asn122 and Arg253 are close to xylose moieties in the -3 subsite, the hypotheses of which were further verified by mutation analysis. In addition, Trp205, Trp132, Tyr372, Tyr277 and Tyr369 in the grove of PbRex8 were found to involve in glucooligosaccharides interactions. This is the first report on a GH family 8 Rex from P. barengoltzii . Conclusions A novel reducing-end xylose-releasing exo-oligoxylanase suitable for xylose production from corncobs was identified, biochemically characterized and structurally elucidated. The properties of PbRex8 may make it an excellent candidate in biorefinery industries. Electronic supplementary material The online version of this article (10.1186/s13068-019-1532-6) contains supplementary material, which is available to authorized users.

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

Cited by 17 publications

References 38 publications

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

Immobilization and Stabilization of Beta-Xylosidases from Penicillium janczewskii

Biochemical characterization of a novel exo-oligoxylanase from Paenibacillus barengoltzii suitable for monosaccharification from corncobs

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