scholarly journals Insight into the Hydrolytic Selectivity of β-Glucosidase to Enhance the Contents of Desired Active Phytochemicals in Medicinal Plants

2018 ◽  
Vol 2018 ◽  
pp. 1-10 ◽  
Author(s):  
Young Soo Kim ◽  
Jin Yeul Ma
Keyword(s):  
Substrate Specificity ◽  
Herbal Medicines ◽  
Glycoside Hydrolase Family ◽  
Enzymatic Conversion ◽  
Herbal Extracts ◽  
Acid Base ◽  
Pharmacologically Active ◽  
Hydrolysis Of ◽  
Hydrolase Family ◽  
Insight Into

Most glycosides in herbal medicines become pharmacologically active after hydrolysis or subsequent metabolism to respective aglycones. Hence, the hydrolytic efficiency of glycosidase is a crucial determinant of the pharmacological efficacy of herbal glycosides. In this study, we investigated the enzymatic conversion of the four herbal extracts and their glycosides using the glycoside hydrolase family 3 β-glucosidase from Lactobacillus antri (rBGLa). We show that β-glucosidase substrate specificity depends on the arrangements and linkage types of sugar residues in glycosides. The enzyme rBGLa showed higher hydrolytic selectivity for glucopyranoside than for glucuronide and rhamnopyranoside, and specificity for 1→6 rather than 1→2 linkages. In addition, in silico 3D structural models suggested that D243 and E426 of rBGLa act as catalytic nucleophile and acid/base residues, respectively. These experiments also suggested that substrate specificity is determined by interactions between the C6 residue of the sugar moiety of the substrate glycoside and the oxygen OD1 of D56 in rBGLa. Therefore, despite the broad substrate spectrum of β-glucosidase, differences in hydrolytic selectivity of β-glucosidases for glycoside structures could be exploited to enhance the hydrolysis of the desired medicinal glycosides in herbs using tailored β-glucosidases, allowing for improvement of specific potencies of herbal medicines.

scholarly journals A novel member of glycoside hydrolase family 30 subfamily 8 with altered substrate specificity

2014 ◽  
Vol 70 (11) ◽  
pp. 2950-2958 ◽  
Author(s):  
Franz J. St John ◽  
Diane Dietrich ◽  
Casey Crooks ◽  
Edwin Pozharski ◽  
Javier M. González ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Biochemical Characterization ◽  
Amino Acid Identity ◽  
Glycoside Hydrolase Family ◽  
High Sequence Identity ◽  
Loop Region ◽  
Hydrolysis Of ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 30

Endoxylanases classified into glycoside hydrolase family 30 subfamily 8 (GH30-8) are known to hydrolyze the hemicellulosic polysaccharide glucuronoxylan (GX) but not arabinoxylan or neutral xylooligosaccharides. This is owing to the specificity of these enzymes for the α-1,2-linked glucuronate (GA) appendage of GX. Limit hydrolysis of this substrate produces a series of aldouronates each containing a single GA substituted on the xylose penultimate to the reducing terminus. In this work, the structural and biochemical characterization of xylanase 30A fromClostridium papyrosolvens(CpXyn30A) is presented. This xylanase possesses a high degree of amino-acid identity to the canonical GH30-8 enzymes, but lacks the hallmark β8–α8 loop region which in part defines the function of this GH30 subfamily and its role in GA recognition.CpXyn30A is shown to have a similarly low activity on all xylan substrates, while hydrolysis of xylohexaose revealed a competing transglycosylation reaction. These findings are directly compared with the model GH30-8 enzyme fromBacillus subtilis, XynC. Despite its high sequence identity to the GH30-8 enzymes,CpXyn30A does not have any apparent specificity for the GA appendage. These findings confirm that the typically conserved β8–α8 loop region of these enzymes influences xylan substrate specificity but not necessarily β-1,4-xylanase function.

scholarly journals Identification and Characterization of a Novel Terrabacter ginsenosidimutans sp. nov. β-Glucosidase That Transforms Ginsenoside Rb1 into the Rare Gypenosides XVII and LXXV

2010 ◽  
Vol 76 (17) ◽  
pp. 5827-5836 ◽  
Author(s):  
Dong-Shan An ◽  
Chang-Hao Cui ◽  
Hyung-Gwan Lee ◽  
Liang Wang ◽  
Sun Chang Kim ◽  
...  
Keyword(s):  
Glycoside Hydrolases ◽  
Glycoside Hydrolase Family ◽  
Ginsenoside Rb1 ◽  
E Coli ◽  
Significant Homology ◽  
Pharmacologically Active ◽  
Hydrolysis Of ◽  
Identification And Characterization ◽  
Hydrolase Family

ABSTRACT A new β-glucosidase from a novel strain of Terrabacter ginsenosidimutans (Gsoil 3082T) obtained from the soil of a ginseng farm was characterized, and the gene, bgpA (1,947 bp), was cloned in Escherichia coli. The enzyme catalyzed the conversion of ginsenoside Rb1 {3-O-[β-d-glucopyranosyl-(1-2)-β-d-glucopyranosyl]-20-O-[β-d-glucopyranosyl-(1-6)-β-d-glucopyranosyl]-20(S)-protopanaxadiol} to the more pharmacologically active rare ginsenosides gypenoside XVII {3-O-β-d-glucopyranosyl-20-O-[β-d-glucopyranosyl-(1-6)-β-d-glucopyranosyl]-20(S)-protopanaxadiol}, gypenoside LXXV {20-O-[β-d-glucopyranosyl-(1-6)-β-d-glucopyranosyl]-20(S)-protopanaxadiol}, and C-K [20-O-(β-d-glucopyranosyl)-20(S)-protopanaxadiol]. A BLAST search of the bgpA sequence revealed significant homology to family 3 glycoside hydrolases. Expressed in E. coli, β-glucosidase had apparent Km values of 4.2 ± 0.8 and 0.14 ± 0.05 mM and V max values of 100.6 ± 17.1 and 329 ± 31 μmol·min−1·mg of protein−1 against p-nitrophenyl-β-d-glucopyranoside and Rb1, respectively. The enzyme catalyzed the hydrolysis of the two glucose moieties attached to the C-3 position of ginsenoside Rb1, and the outer glucose attached to the C-20 position at pH 7.0 and 37°C. These cleavages occurred in a defined order, with the outer glucose of C-3 cleaved first, followed by the inner glucose of C-3, and finally the outer glucose of C-20. These results indicated that BgpA selectively and sequentially converts ginsenoside Rb1 to the rare ginsenosides gypenoside XVII, gypenoside LXXV, and then C-K. Herein is the first report of the cloning and characterization of a novel ginsenoside-transforming β-glucosidase of the glycoside hydrolase family 3.

The Pseudomonas cellulosa glycoside hydrolase family 51 arabinofuranosidase exhibits wide substrate specificity

2001 ◽  
Vol 358 (3) ◽  
pp. 607-614 ◽  
Author(s):  
Marie-Helene BEYLOT ◽  
Vincent A. McKIE ◽  
Alphons G. J. VORAGEN ◽  
Chantal H. L. DOESWIJK-VORAGEN ◽  
Harry J. GILBERT
Keyword(s):  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Genomic Dna ◽  
Biochemical Properties ◽  
Glycoside Hydrolase Family ◽  
Acid Base ◽  
Membrane Bound ◽  
Hydrolase Family ◽  
Glycoside Hydrolase Family 51 ◽  
Wide Substrate Specificity

To investigate the mechanism by which Pseudomonas cellulosa releases arabinose from polysaccharides and oligosaccharides, a gene library of P. cellulosa genomic DNA was screened for 4-methylumbelliferyl-α-l-arabinofuranosidase (MUAase) activity. A single MUAase gene (abf51A) was isolated, which encoded a non-modular glycoside hydrolase family (GH) 51 arabinofuranosidase (Abf51A) of 57000Da. The substrate specificity of the Abf51A showed that it preferentially removed α1,2- and α1,3-linked arabinofuranose side chains from either arabinan or arabinoxylan, and hydrolysed α1,5-linked arabino-oligosaccharides, although at a much lower rate. The activity of Abf51A against arabinoxylan was similar to a GH62 arabinofuranosidase encoded by a P. cellulosa gene. Glu-194 and Glu-321 of Abf51A are conserved in GH51 enzymes, and it has been suggested that these amino acids comprise the key catalytic acid/base and nucleophile residues, respectively. To evaluate this hypothesis the biochemical properties of E194A and E321A mutants of Abf51A were evaluated. The data were consistent with the view that Glu-194 and Glu-321 comprise the key catalytic residues of Abf51A. These data, in conjunction with the results presented in the accompanying paper [Beylot, Emami, McKie, Gilbert and Pell (2001) Biochem. J. 358, 599–605], indicate that P. cellulosa expresses a membrane-bound GH51 arabinofuranosidase that plays a pivotal role in releasing arabinose from a range of polysaccharides and oligosaccharides.

scholarly journals Characterization of Glycoside Hydrolase Family 5 Proteins in Schizosaccharomyces pombe

2010 ◽  
Vol 9 (11) ◽  
pp. 1650-1660 ◽  
Author(s):  
Encarnación Dueñas-Santero ◽  
Ana Belén Martín-Cuadrado ◽  
Thierry Fontaine ◽  
Jean-Paul Latgé ◽  
Francisco del Rey ◽  
...  
Keyword(s):  
Cell Wall ◽  
Schizosaccharomyces Pombe ◽  
Protein Characterization ◽  
Wall Material ◽  
Glycoside Hydrolase Family ◽  
Content Type ◽  
Hydrolysis Of ◽  
Controlled Hydrolysis ◽  
Hydrolase Family

ABSTRACT In yeast, enzymes with β-glucanase activity are thought to be necessary in morphogenetic events that require controlled hydrolysis of the cell wall. Comparison of the sequence of the Saccharomyces cerevisiae exo-β(1,3)-glucanase Exg1 with the Schizosaccharomyces pombe genome allowed the identification of three genes that were named exg1 + (locus SPBC1105.05), exg2 + (SPAC12B10.11), and exg3 + (SPBC2D10.05). The three proteins have different localizations: Exg1 is secreted to the periplasmic space, Exg2 is a membrane protein, and Exg3 is a cytoplasmic protein. Characterization of the biochemical activity of the proteins indicated that Exg1 and Exg3 are active only against β(1,6)-glucans while no activity was detected for Exg2. Interestingly, Exg1 cleaves the glucans with an endohydrolytic mode of action. exg1 + showed periodic expression during the cell cycle, with a maximum coinciding with the septation process, and its expression was dependent on the transcription factor Sep1. The Exg1 protein localizes to the septum region in a pattern that was different from that of the endo-β(1,3)-glucanase Eng1. Overexpression of Exg2 resulted in an increase in cell wall material at the poles and in the septum, but the putative catalytic activity of the protein was not required for this effect.

scholarly journals Structure of a bacterial glycoside hydrolase family 63 enzyme in complex with its glycosynthase product, and insights into the substrate specificity

FEBS Journal ◽  
2013 ◽  
Vol 280 (18) ◽  
pp. 4560-4571 ◽  
Author(s):  
Takatsugu Miyazaki ◽  
Megumi Ichikawa ◽  
Gaku Yokoi ◽  
Motomitsu Kitaoka ◽  
Haruhide Mori ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Hydrolase Family

scholarly journals Substrate Specificity in Glycoside Hydrolase Family 10

2000 ◽  
Vol 275 (30) ◽  
pp. 23020-23026 ◽  
Author(s):  
Valérie Ducros ◽  
Simon J. Charnock ◽  
Urszula Derewenda ◽  
Zygmunt S. Derewenda ◽  
Zbigniew Dauter ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Glycoside Hydrolase ◽  
Glycoside Hydrolase Family ◽  
Glycoside Hydrolase Family 10 ◽  
Hydrolase Family

scholarly journals Study of the mode of action of a polygalacturonase from the phytopathogen Burkholderia cepacia

2007 ◽  
Vol 407 (2) ◽  
pp. 207-217 ◽  
Author(s):  
Claudia Massa ◽  
Mads H. Clausen ◽  
Jure Stojan ◽  
Doriano Lamba ◽  
Cristiana Campa
Keyword(s):  
Mode Of Action ◽  
Burkholderia Cepacia ◽  
Time Course ◽  
Glycoside Hydrolase Family ◽  
Enzymatic Mechanism ◽  
Processive Enzyme ◽  
Chain Lengths ◽  
Methylation Patterns ◽  
Hydrolysis Of ◽  
Hydrolase Family

We have recently isolated and heterologously expressed BcPeh28A, an endopolygalacturonase from the phytopathogenic Gram-negative bacterium Burkholderia cepacia. Endopolygalacturonases belong to glycoside hydrolase family 28 and are responsible for the hydrolysis of the non-esterified regions of pectins. The mode of action of BcPeh28A on different substrates has been investigated and its enzymatic mechanism elucidated. The hydrolysis of polygalacturonate indicates that BcPeh28A is a non-processive enzyme that releases oligomers with chain lengths ranging from two to eight. By inspection of product progression curves, a kinetic model has been generated and extensively tested. It has been used to derive the kinetic parameters that describe the time course of the formation of six predominant products. Moreover, an investigation of the enzymatic activity on shorter substrates that differ in their overall length and methylation patterns sheds light on the architecture of the BcPeh28A active site. Specifically the tolerance of individual sites towards methylated saccharide units was rationalized on the basis of the hydrolysis of hexagalacturonides with different methylation patterns.

Nanomaterials for the delivery of Herbal Bioactive Compounds

2021 ◽  
Vol 17 ◽  
Author(s):  
Shadma Wahab ◽  
Md. Parwez Ahmad ◽  
Arshad Hussain ◽  
Shaik Fayazuddin Abdul Qadir
Keyword(s):  
Drug Delivery ◽  
Bioactive Compounds ◽  
Targeted Drug Delivery ◽  
Herbal Medicines ◽  
Herbal Drugs ◽  
Herbal Extracts ◽  
Significant Component ◽  
Pharmaceutical Application ◽  
Low Solubility ◽  
Insight Into

: Nanotechnology is a multidisciplinary domain that involves overlapping of areas such as nonanomaterials, nanoelectronics, and nanobiotechnology. Herbal medicine is a significant component of traditional medicine and has been a treatment part of many diseases. Asian peoples are using these herbal medicines for decades. Still, herbal extracts' therapeutic efficacy and pharmaceutical application are associated with many factors such as poor bioavailability, low solubility, permeability, and lack of targeting potential. In the present work, we have reviewed thriving strategies for the targeted drug delivery of phytoconstituents and critically explain the most recent progressions on emerging novel nanophytomedicine-based materials as herbal medicines carriers. Nanotechnology-based clinical trial studies targeting herbal bioactive compounds were discussed. Advancements in nanotechnology-based drug delivery systems intended to enhance cellular uptake, improved pharmacokinetics and effectiveness of herbal drugs have facilitated the powerful targeting of specific agents against diseases. This review provides insight into current progress and future opportunities for nanomedicines as potential curative targets for the delivery of herbal bioactive compounds. This information could be used as platforms for the future expansion of multi-functional nano constructs for the advanced detection of diseases and functional drug delivery of phytoconstituents.

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