Heterologous Expression and Characterization of a Glycoside Hydrolase Family 45 endo-β-1,4-Glucanase from a Symbiotic Protist of the Lower Termite, Reticulitermes speratus

2013 ◽  
Vol 169 (6) ◽  
pp. 1910-1918 ◽  
Author(s):  
Masato Otagiri ◽  
Crisanto M. Lopez ◽  
Katsuhiko Kitamoto ◽  
Manabu Arioka ◽  
Toshiaki Kudo ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Reticulitermes Speratus ◽  
Lower Termite ◽  
Hydrolase Family ◽  
Symbiotic Protist

Heterologous Expression and Characterization of an Endoglucanase from a Symbiotic Protist of the Lower Termite, Reticulitermes speratus

2009 ◽  
Vol 160 (4) ◽  
pp. 1168-1178 ◽  
Author(s):  
Nemuri Todaka ◽  
Crisanto M. Lopez ◽  
Tetsushi Inoue ◽  
Kanako Saita ◽  
Jun-ichi Maruyama ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Reticulitermes Speratus ◽  
Lower Termite ◽  
Symbiotic Protist

Heterologous expression and characterization of a novel glycoside hydrolase family 55 β-1,3-glucanase, AcGluA, from Archangium sp. strain AC19

2021 ◽  
Vol 105 (18) ◽  
pp. 6793-6803
Author(s):  
Yanxin Wang ◽  
Ding Li ◽  
Chaonan Dong ◽  
Yuqiang Zhao ◽  
Lei Zhang ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family

scholarly journals Characterization of Fusarium oxysporum β-1,6-Galactanase, an Enzyme That Hydrolyzes Larch Wood Arabinogalactan

2007 ◽  
Vol 73 (9) ◽  
pp. 3109-3112 ◽  
Author(s):  
Tatsuji Sakamoto ◽  
Yuya Taniguchi ◽  
Shiho Suzuki ◽  
Hideshi Ihara ◽  
Haruhiko Kawasaki
Keyword(s):  
Fusarium Oxysporum ◽  
Glycoside Hydrolase ◽  
Recombinant Enzyme ◽  
Glycoside Hydrolase Family ◽  
Type Ii ◽  
High Similarity ◽  
Degrading Enzyme ◽  
Larch Wood ◽  
Hydrolase Family

ABSTRACT A type II arabinogalactan-degrading enzyme (FoGal1) was purified from Fusarium oxysporum 12S, and the corresponding cDNA was isolated. FoGal1 had high similarity to enzymes of glycoside hydrolase family 5. Treatment of larch wood arabinogalactan with the recombinant enzyme indicated that FoGal1 is a β-1,6-galactanase that preferentially debranches β-1,6-galactobiose from the substrate.

scholarly journals Biochemical characterization of a glycoside hydrolase family 43 β-D-galactofuranosidase from the fungus Aspergillus niger

2021 ◽  
Author(s):  
Gregory S Bulmer ◽  
Fang Wei Yuen ◽  
Naimah Begum ◽  
Bethan S Jones ◽  
Sabine S Flitsch ◽  
...  
Keyword(s):  
Aspergillus Niger ◽  
Glycoside Hydrolase ◽  
Biochemical Characterization ◽  
Maximum Activity ◽  
Glycoside Hydrolase Family ◽  
Enzyme Specificity ◽  
Fungal Enzymes ◽  
Glycoside Hydrolase Family 43 ◽  
Hydrolase Family

β-D-Galactofuranose (Galf) and its polysaccharides are found in bacteria, fungi and protozoa but do not occur in mammalian tissues, and thus represent a specific target for anti-pathogenic drugs. Understanding the enzymatic degradation of these polysaccharides is therefore of great interest, but the identity of fungal enzymes with exclusively galactofuranosidase activity has so far remained elusive. Here we describe the identification and characterization of a galactofuranosidase from the industrially important fungus Aspergillus niger. Phylogenetic analysis of glycoside hydrolase family 43 subfamily 34 (GH43_34) members revealed the occurrence of three distinct clusters and, by comparison with specificities of characterized bacterial members, suggested a basis for prediction of enzyme specificity. Using this rationale, in tandem with molecular docking, we identified a putative β-D-galactofuranosidase from A. niger which was recombinantly expressed in Escherichia coli. The Galf-specific hydrolase, encoded by xynD demonstrates maximum activity at pH 5, 25 °C towards 4-Nitrophenyl-β-galactofuranoside (pNP-βGalf), with a Km of 17.9 ± 1.9 mM and Vmax of 70.6 ± 5.3 μmol min-1. The characterization of this first fungal GH43 galactofuranosidase offers further molecular insight into the degradation of Galf-containing structures and may inform clinical treatments against fungal pathogens.

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