83058-47-3Relevant articles and documents
Characterization of Two New Endo-β-1,4-xylanases from Eupenicillium parvum 4–14 and Their Applications for Production of Feruloylated Oligosaccharides
Long, Liangkun,Xu, Meijuan,Shi, Yuexin,Lin, Qunying,Wang, Jing,Ding, Shaojun
, p. 816 - 833 (2018/05/15)
Two new endo-1,4-beta-xylanases encoding genes EpXyn1 and EpXyn3 were isolated from mesophilic fungus Eupenicillium parvum 4–14. Based on analysis of catalytic domain and phylogenetic trees, the xylanases EpXYN1 (404 aa) and EpXYN3 (220 aa) belong to glycoside hydrolase (GH) family 10 and 11, respectively. Both EpXYN1 and EpXYN3 were successfully expressed in Pichia pastoris and the recombinant enzymes were characterized using beechwood xylan, birchwood xylan, or oat spelt xylan as substrates, respectively. The optimum temperatures and pH values were 75?°C and 5.5 for EpXYN1, and 55?°C and 5.0 for EpXYN3. EpXYN1 exhibited a high stability at high temperature (65?°C) or at pH values from 8 to 10. EpXYN3 kept over 80% enzymatic activity after treatment at pH values from 3 to 10. The specific activities of EpXYN1 and EpXYN3 were 384.42 and 214.20?U/mg?using beechwood xylan as substrate, respectively. EpXYN1 showed lower Km values and higher specific activities toward different xylans compared to EpXYN3. Thin-layer chromatography analysis indicated that the hydrolysis profiles of xylans or xylo-oligosacharides were different by EpXYN1and EpXYN3. EpXYN3 had a higher efficiency than EpXYN1 in production of feruloylated oligosaccharides (FOs) from de-starched wheat bran. The maximum levels of FOs released by EpXYN1 and EpXYN3 were 11.1 and 14.4?μmol/g, respectively. In conclusion, the two xylanases are potential candidates for various industrial applications.
Purification, characterization and mass spectrometric identification of two thermophilic xylanases from Sporotrichum thermophile
Vafiadi, Christina,Christakopoulos, Paul,Topakas, Evangelos
experimental part, p. 419 - 424 (2011/10/31)
Two xylanases were purified to electrophoretic homogeneity from the thermophilic fungus Sporotrichum thermophile grown in a submerged liquid culture using wheat straw as carbon source. The enzymes, StXyn1 and StXyn2, have molecular masses of 24 kDa and 48 kDa, respectively, and are optimally active at pH 5 and at 60 °C. Both enzymes displayed remarkable stability up to 50 °C for 1 h, exhibiting a half-life of 60 min (StXyn1) and 115 min (StXyn2) at 60 °C. Biochemical characterization of the two xylanases against poly- and oligosaccharides indicated that StXyn1 and StXyn2 hydrolytic profiles match those of xylanase family 11 and family 10, respectively. LC-MS/MS analysis provided peptide mass and sequence information that assisted the identification of the corresponding xylanase genes from the S. thermophile genome and the classification of the two purified StXyn1 and StXyn2 as a family GH11 and GH10 endo-1,4-β-xylanases, respectively.
Hydrolysis of (1->3)- and (1->2)-β-D-xylosidic linkages by an endo-(1->4)-β-D-xylanase of Cryptococcus albidus
Vrsanska, Maria,Hirsch, Jan,Kovac, Pavol,Biely, Peter
, p. 251 - 256 (2007/10/02)
The substrate specificity of an endo-(1->4)-β-D-xylanase of the yeast Cryptococcus albidus was investigated using a series of methyl β-D-xylotriosides.In addition to (1->4) linkages, the enzyme could cleave (1->3) and (1->2) linkages adjacent to a (1->4) linkage and further from the non-reducing end of the substrate.The enzyme could hydrolyse a (1->3) linkage that attached a terminal xylopyranosyl group to a (1->4)-linked xylobiosyl moiety.The enzyme did not attack α-D-xylosidic linkages.The rate of cleavage of (1->4) linkages was much higher than those of other linkages at 0.5 mM substrate, but the rates were comparable at 20 mM substrate when transglycosylation reactions also occurred that facilitated degradation of the substrates.
