Purification, Identification, and Characterization of a Glycoside Hydrolase Family 11-Xylanase with High Activity from Aspergillus niger VTCC 017

2021 ◽  
Author(s):  
Thi Mai Anh Dao ◽  
Nguyen Tien Cuong ◽  
Thi Trung Nguyen ◽  
Nguyen Phuong Dai Nguyen ◽  
Do Thi Tuyen
Keyword(s):  
Aspergillus Niger ◽  
High Activity ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Identification And Characterization ◽  
Hydrolase Family

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.

scholarly journals Identification and Characterization of a Mucilaginibacter sp. Strain QM49 β-Glucosidase and Its Use in the Production of the Pharmaceutically Active Minor Ginsenosides (S)-Rh1and (S)-Rg2

2013 ◽  
Vol 79 (19) ◽  
pp. 5788-5798 ◽  
Author(s):  
Chang-Hao Cui ◽  
Qing-Mei Liu ◽  
Jin-Kwang Kim ◽  
Bong-Hyun Sung ◽  
Song-Gun Kim ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Vector System ◽  
Glycoside Hydrolase Family ◽  
Scale Production ◽  
Amino Acid Residues ◽  
Content Type ◽  
Silica Column ◽  
Identification And Characterization ◽  
Hydrolase Family

ABSTRACTHere, we isolated and characterized a new ginsenoside-transforming β-glucosidase (BglQM) fromMucilaginibactersp. strain QM49 that shows biotransformation activity for various major ginsenosides. The gene responsible for this activity,bglQM, consists of 2,346 bp and is predicted to encode 781 amino acid residues. This enzyme has a molecular mass of 85.6 kDa. Sequence analysis of BglQM revealed that it could be classified into glycoside hydrolase family 3. The enzyme was overexpressed inEscherichia coliBL21(DE3) using a maltose binding protein (MBP)-fused pMAL-c2x vector system containing the tobacco etch virus (TEV) proteolytic cleavage site. Overexpressed recombinant BglQM could efficiently transform the protopanaxatriol-type ginsenosides Re and Rg1into (S)-Rg2and (S)-Rh1, respectively, by hydrolyzing one glucose moiety attached to the C-20 position at pH 8.0 and 30°C. TheKmvalues forp-nitrophenyl-β-d-glucopyranoside, Re, and Rg1were 37.0 ± 0.4 μM and 3.22 ± 0.15 and 1.48 ± 0.09 mM, respectively, and theVmaxvalues were 33.4 ± 0.6 μmol min−1mg−1of protein and 19.2 ± 0.2 and 28.8 ± 0.27 nmol min−1mg−1of protein, respectively. A crude protopanaxatriol-type ginsenoside mixture (PPTGM) was treated with BglQM, followed by silica column purification, to produce (S)-Rh1and (S)-Rg2at chromatographic purities of 98% ± 0.5% and 97% ± 1.2%, respectively. This is the first report of gram-scale production of (S)-Rh1and (S)-Rg2from PPTGM using a novel ginsenoside-transforming β-glucosidase of glycoside hydrolase family 3.

Identification and Characterization of a Glycoside Hydrolase Family 9 Member from the Digestive Gland of the Snail Achatina fulica

2021 ◽  
Author(s):  
Youssef Bacila Sade ◽  
Camila Silva Gonçalves ◽  
Sandra Mara Naressi Scapin ◽  
Guilherme Luiz Pinheiro ◽  
Roberto Becht Flatschart ◽  
...  
Keyword(s):  
Digestive Gland ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Achatina Fulica ◽  
Glycoside Hydrolase Family 9 ◽  
Identification And Characterization ◽  
Hydrolase Family

scholarly journals Biochemical characterization of Aspergillus niger CfcI, a glycoside hydrolase family 18 chitinase that releases monomers during substrate hydrolysis

Microbiology ◽  
2012 ◽  
Vol 158 (8) ◽  
pp. 2168-2179 ◽  
Author(s):  
Jolanda M. van Munster ◽  
Rachel M. van der Kaaij ◽  
Lubbert Dijkhuizen ◽  
Marc J. E. C. van der Maarel
Keyword(s):  
Aspergillus Niger ◽  
Glycoside Hydrolase ◽  
Biochemical Characterization ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family ◽  
Substrate Hydrolysis

scholarly journals The thermostable 4,6-α-glucanotransferase of Bacillus coagulans DSM 1 synthesizes isomaltooligosaccharides

Amylase ◽  
2021 ◽  
Vol 5 (1) ◽  
pp. 13-22
Author(s):  
Gang Xiang ◽  
Piet L. Buwalda ◽  
Marc J.E.C van der Maarel ◽  
Hans Leemhuis
Keyword(s):  
Bacillus Coagulans ◽  
Glycoside Hydrolase Family ◽  
Rat Intestine ◽  
Glycaemic Response ◽  
Food Ingredient ◽  
Starch Conversion ◽  
Identification And Characterization ◽  
Hydrolase Family

Abstract The 4,6-α-glucanotransferases of the glycoside hydrolase family 70 can convert starch into isomaltooligosaccharides (IMOs). However, no thermostable 4,6-α-glucanotransferases have been reported to date, limiting their applicability in the starch conversion industry. Here we report the identification and characterization of a thermostable 4,6-α-glucanotransferase from Bacillus coagulans DSM 1. The gene was cloned and the recombinant protein, called BcGtfC, was produced in Escherichia coli. BcGtfC is stable up to 66 °C in the presence of substrate. It converts debranched starch into an IMO product with a high percentage of α-1,6-glycosidic linkages and a relatively high molecular weight compared to commercially available IMOs. Importantly, the product is only partly and very slowly digested by rat intestine powder, suggesting that the IMO will provide a low glycaemic response in vivo when applied as food ingredient. Thus, BcGtfC is a thermostable 4,6-α-glucanotransferase suitable for the industrial production of slowly digestible IMOs from starch.

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.

Characterization of a Theme C Glycoside Hydrolase Family 9 Endo-Beta-Glucanase from a Biogas Reactor Metagenome

2018 ◽  
Vol 37 (5) ◽  
pp. 454-460
Author(s):  
Carola Schröder ◽  
Christin Burkhardt ◽  
Philip Busch ◽  
Georg Schirrmacher ◽  
Jörg Claren ◽  
...  
Keyword(s):  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Beta Glucanase ◽  
Glycoside Hydrolase Family 9 ◽  
Biogas Reactor ◽  
Hydrolase Family

Cloning, Expression and Characterization of a Glycoside Hydrolase Family 39 Xylosidase from Bacillus Halodurans C-125

2007 ◽  
pp. 189-198
Author(s):  
Kurt Wagschal ◽  
Diana Franqui-Espiet ◽  
Charles C. Lee ◽  
George H. Robertson ◽  
Dominic W. S. Wong
Keyword(s):  
Glycoside Hydrolase ◽  
Bacillus Halodurans ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family
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