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|Storage Temperature:||Below -10oC|
|Stability:||> 10 years under recommended storage conditions|
|Substrate For (Enzyme):||endo-1,4-β-Xylanase, α-Glucuronidase|
High purity 23-(4-O-Methyl-α-D-Glucuronyl)-xylotriose for use in research, biochemical enzyme assays and in vitro diagnostic analysis.
(Trichoderma longibrachiatum) E-XYAN4 - endo-1,4-β-Xylanase M4 (Aspergillus niger) E-XYRU6 - endo-1,4-β-Xylanase (rumen microorganism) E-XYNBS - endo-1,4-β-Xylanase
(Bacillus stearothermophilus T6) E-XYNACJ - endo-1,4-β-Xylanase (Cellvibrio japonicus) E-XYLNP - endo-1,4-β-Xylanase (Neocallimastix patriciarum) E-XYLATM - endo-1,4-β-Xylanase (Thermotoga maritima)
Xylanase from marine filamentous fungus Pestalotiopsis sp. AN-7 was activated with diluted salt solution like brackish water.
Koh, S., Mizuno, M., Izuoka, Y., Fujino, N., Hamada-Sato, N. & Amano, Y. (2021). Journal of Applied Glycoscience, 68(1), 11-18.
The genus Pestalotiopsis are endophytic fungi that have recently been identified as cellulolytic system producers. We herein cloned a gene coding for a xylanase belonging to glycoside hydrolase (GH) family 10 (PesXyn10A) from Pestalotiopsis sp. AN-7, which was isolated from the soil of a mangrove forest. This protein was heterologously expressed by Pichia pastoris as a host, and its enzymatic properties were characterized. PesXyn10A was produced as a glycosylated protein and coincident to theoretical molecular mass (35.3 kDa) after deglycosylation by peptide-N-glycosidase F. Purified recombinant PesXyn10A exhibited maximal activity at pH 6.0 and 50°C, and activity was maintained at 90 % at pH 5.0 and temperatures lower than 30°C for 24 h. The substrate specificity of PesXyn10A was limited and it hydrolyzed glucuronoxylan and arabinoxylan, but not β-glucan. The final hydrolysis products from birchwood xylan were xylose, xylobiose, and 1,23-α-D-(4-O-methyl-glucuronyl)-1,4-β-D-xylotriose. The addition of metallic salts (NaCl, KCl, MgCl2, and CaCl2) activated PesXyn10A for xylan degradation, and maximal activation by these divalent cations was approximately 160% at a concentration of 5 mM. The thermostability of PesXyn10A significantly increased in the presence of 50 mM NaCl or 5 mM MgCl2. The present results suggest that the presence of metallic salts at a low concentration, similar to brackish water, exerts positive effects on the enzyme activity and thermal stability of PesXyn10A.Hide Abstract