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==Crystal Structure of AHE enzyme from Alicyclobacillus herbarius== | ==Crystal Structure of AHE enzyme from Alicyclobacillus herbarius== | ||
<StructureSection load='6yn7' size='340' side='right'caption='[[6yn7]]' scene=''> | <StructureSection load='6yn7' size='340' side='right'caption='[[6yn7]], [[Resolution|resolution]] 1.98Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YN7 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6yn7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Alicyclobacillus_herbarius Alicyclobacillus herbarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6YN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6YN7 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6yn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yn7 OCA], [https://pdbe.org/6yn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yn7 RCSB], [https://www.ebi.ac.uk/pdbsum/6yn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yn7 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.98Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6yn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6yn7 OCA], [https://pdbe.org/6yn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6yn7 RCSB], [https://www.ebi.ac.uk/pdbsum/6yn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6yn7 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
beta-Glucosidases are used in the food industry to hydrolyse glycosidic bonds in complex sugars, with enzymes sourced from extremophiles better able to tolerate the process conditions. In this work, a novel beta-glycosidase from the acidophilic organism Alicyclobacillus herbarius was cloned and heterologously expressed in Escherichia coli BL21(DE3). AheGH1 was stable over a broad range of pH values (5-11) and temperatures (4-55 degrees C). The enzyme exhibited excellent tolerance to fructose and good tolerance to glucose, retaining 65 % activity in the presence of 10 % (w/v) glucose. It also tolerated organic solvents, some of which appeared to have a stimulating effect, in particular ethanol with a 1.7-fold increase in activity at 10 % (v/v). The enzyme was then applied for the cleavage of isoflavone from isoflavone glucosides in an ethanolic extract of soy flour, to produce soy isoflavones, which constitute a valuable food supplement, full conversion was achieved within 15 min at 30 degrees C. | |||
Release of Soybean Isoflavones by Using a beta-Glucosidase from Alicyclobacillus herbarius.,Delgado L, Heckmann CM, Di Pisa F, Gourlay L, Paradisi F Chembiochem. 2020 Nov 25. doi: 10.1002/cbic.202000688. PMID:33237595<ref>PMID:33237595</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6yn7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-glucosidase 3D structures|Beta-glucosidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Alicyclobacillus herbarius]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Di Pisa F]] | [[Category: Di Pisa F]] | ||
[[Category: Gourlay LJ]] | [[Category: Gourlay LJ]] | ||
Latest revision as of 16:31, 24 January 2024
Crystal Structure of AHE enzyme from Alicyclobacillus herbariusCrystal Structure of AHE enzyme from Alicyclobacillus herbarius
Structural highlights
Publication Abstract from PubMedbeta-Glucosidases are used in the food industry to hydrolyse glycosidic bonds in complex sugars, with enzymes sourced from extremophiles better able to tolerate the process conditions. In this work, a novel beta-glycosidase from the acidophilic organism Alicyclobacillus herbarius was cloned and heterologously expressed in Escherichia coli BL21(DE3). AheGH1 was stable over a broad range of pH values (5-11) and temperatures (4-55 degrees C). The enzyme exhibited excellent tolerance to fructose and good tolerance to glucose, retaining 65 % activity in the presence of 10 % (w/v) glucose. It also tolerated organic solvents, some of which appeared to have a stimulating effect, in particular ethanol with a 1.7-fold increase in activity at 10 % (v/v). The enzyme was then applied for the cleavage of isoflavone from isoflavone glucosides in an ethanolic extract of soy flour, to produce soy isoflavones, which constitute a valuable food supplement, full conversion was achieved within 15 min at 30 degrees C. Release of Soybean Isoflavones by Using a beta-Glucosidase from Alicyclobacillus herbarius.,Delgado L, Heckmann CM, Di Pisa F, Gourlay L, Paradisi F Chembiochem. 2020 Nov 25. doi: 10.1002/cbic.202000688. PMID:33237595[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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