A new xylanase (XYL2) was purified from solid-state cultures of Trichoderma harzianum strain C by ultrafiltration and gel filtration. SDS-PAGE of the xylanase showed an apparent homogeneity and molecular weight of 18 kDa. It had the highest activity at pH 5.0 and 45 degrees C and was stable at 50 degrees C and pH 5.0 up to 4 h xylanase. XYL2 had a low Km with insoluble oat spelt xylan as substrate. Compared to the amino acid composition of xylanases from Trichoderma spp, xylanase XYL2 presented a high content of glutamate/glutamine, phenylalanine and cysteine, and a low content of serine. Xylanase XYL2 improved the delignification and selectivity of unbleached hardwood kraft pulp.
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http://dx.doi.org/10.1038/sj.jim.2900682 | DOI Listing |
Appl Biochem Biotechnol
April 2024
Laboratoire de Microbiologie Appliquée, Faculté Des Sciences de La Nature Et de La Vie, Université de Bejaia, 06000, Bejaia, Algeria.
Xylanase production by Streptomyces sp. S1M3I was optimized by response surface methodology (RSM), followed by a partial characterization of these enzymes. Olive pomace was used as a substrate for growing Streptomyces sp.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
January 2021
Institute of Chemistry, Slovak Academy of Sciences, Dúbravská cesta 9, 845 38, Bratislava, Slovakia.
Typical bacterial GH30 xylanases are glucuronoxylanases requiring 4-O-methylglucuronic acid (MeGlcA) substitution of a xylan main chain for their action. They do not exhibit a significant activity on neutral xylooligosaccharides, arabinoxylan (AraX), or rhodymenan (Rho). In this work, the biochemical characterization of the bacterial Clocl_1795 xylanase from Hungateiclostridium (Clostridium) clariflavum DSM 19732 (HcXyn30A) is presented.
View Article and Find Full Text PDFMicrob Cell Fact
September 2019
State Key Laboratory of Agrobiotechnology, College of Biological Sciences, China Agricultural University, Beijing, 100193, China.
Background: Xylanases randomly cleave the internal β-1,4-glycosidic bonds in the xylan backbone and are grouped into different families in the carbohydrate-active enzyme (CAZy) database. Although multiple xylanases are detected in single strains of many filamentous fungi, no study has been reported on the composition, synergistic effect, and mode of action in a complete set of xylanases secreted by the same microorganism.
Results: All three xylanases secreted by Penicillium chrysogenum P33 were expressed and characterized.
Int J Biol Macromol
July 2019
Department of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, PO BOX 1334, Durban 4000, South Africa. Electronic address:
This work is the first report on the isolation and structural elucidation of xylan from bambara and cowpea biomass. The xylans, isolated using acidic delignification followed by NaOH extraction method gave 12.3% and 13.
View Article and Find Full Text PDFFood Chem
April 2017
Department of Biological Sciences, Universidade Estadual de Santa Cruz, 45662-900 Ilhéus, Bahia, Brazil. Electronic address:
The enzymes Xyl1 and Xyl2 from T. stromaticum were purified and identified by mass spectrometry (MALDI-TOF/MS). Xyl1 contained three proteins with similarity to xylanase family 10, 62 and anarabinofuranosidase of the Trichoderma genus and Xyl2 contained a protein with similarity to endo-1,4-β-xylanase.
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