Characterization of two extracellular β-glucosidases produced from the cellulolytic fungus Aspergillus sp. YDJ216 and their potential applications for the hydrolysis of flavone glycosides

Oh, Jong Min; Lee, Jae Pil; Baek, Seung Cheol; Kim, Seul Gi; Jo, Yang Do; Kim, Jungho; Kim, Hoon

doi:10.1016/j.ijbiomac.2018.01.020

Cited by 21 publications

(18 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Mallerman et al worked on Flammulina velutipes CFK 3111, a white rot fungus, and observed the maximal β-glucosidase production of 1.6 U/mLwith a glucose production of ~10 g/L [87]. In a study, Jongmin et al isolated Aspergillus sp.YDJ216, which produced two β-glucosidases, BGL1 and BGL2, and out of these two, BGL1 exhibited the maximum activity (953.2 U/mg) [88]. Abdella et al worked on A. niger , and found the maximum BGL production at the repeated batch mode in the rotating fibrous bed bioreactor (RFBB) of about 1.78 U/mL/day [59].…”

Section: Industrial Importance Of β-Glucosidase In Biofuelsmentioning

confidence: 99%

Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application

et al. 2019

View full text Add to dashboard Cite

The biomass to biofuels production process is green, sustainable, and an advanced technique to resolve the current environmental issues generated from fossil fuels. The production of biofuels from biomass is an enzyme mediated process, wherein β-glucosidase (BGL) enzymes play a key role in biomass hydrolysis by producing monomeric sugars from cellulose-based oligosaccharides. However, the production and availability of these enzymes realize their major role to increase the overall production cost of biomass to biofuels production technology. Therefore, the present review is focused on evaluating the production and efficiency of β-glucosidase enzymes in the bioconversion of cellulosic biomass for biofuel production at an industrial scale, providing its mechanism and classification. The application of BGL enzymes in the biomass conversion process has been discussed along with the recent developments and existing issues. Moreover, the production and development of microbial BGL enzymes have been explained in detail, along with the recent advancements made in the field. Finally, current hurdles and future suggestions have been provided for the future developments. This review is likely to set a benchmark in the area of cost effective BGL enzyme production, specifically in the biorefinery area.

show abstract

Section: Industrial Importance Of β-Glucosidase In Biofuelsmentioning

confidence: 99%

Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application

et al. 2019

View full text Add to dashboard Cite

show abstract

“…Purification of the enzyme Crude enzyme preparation was performed as previously described [13]. The crude enzyme was loaded onto a Sephacryl S-200 HR column (HiPrep 16/60) after dialysis against 50 mM sodium phosphate buffer (pH 7.2) containing 150 mM NaCl [14]. The protein was eluted at a flow rate of 0.5 mL/min.…”

Section: Esterase Assaymentioning

confidence: 99%

Characterization of an alkaline esterase from an enriched metagenomic library derived from an oil-spill area

Baek

Lee

et al. 2019

JABC

Self Cite

View full text Add to dashboard Cite

A novel esterase gene (est7S) was cloned from an enriched metagenomic library derived from an oil-spill area. The gene encoded a protein of 505 amino acids, and the molecular mass of the Est7S was estimated to be 54,512 Da with no signal peptide. Est7S showed the highest identity of 40% to an esterase from a sludge metagenome compared to the characterized enzymes with their properties, although it showed 99% identity to a carboxylesterase in the genome sequence of Alcanivorax borkumensis SK2. Est7S had catalytic triad residues, Ser183, Glu312, and His420, and the GESAG motif in most family VII lipolytic enzymes. Est7S was purified from the crude extract of clone SM7 using Sephacryl S-200 HR and HiTrap Q column chromatographies. The purified Est7S was optimally active at 50 o C and pH 10.0. Est7S showed a high specific activity of 366.7 U/mg protein. It preferred short length esters, particularly p-nitrophenyl acetate, efficiently hydrolyzed R-and S-enantiomers of methyl-3-hydroxy-2-methylpropionate, and glyceryl tributyrate. These properties of Est7S may provide potential merits in biotechnological applications such as detergent and paper processing under alkaline conditions.

show abstract

“…A compost sample was obtained from the Compost Factory [22], and cellulolytic fungi were isolated on PDA (potato dextrose agar) plates containing 0.4% CMC (PDA/CMC) or xylan (PDA/ xylan), as described previously [15]. Based on the halo size around the colony, a strain was selected and named YDJ14.…”

Section: Isolation and Identification Of The Fungal Strainmentioning

confidence: 99%

“…The isolate was cultured at 30 o C, with shaking at 150 rpm in 200 ml of potato dextrose broth, as described previously [15], with some modifications (i.e., 21 days of culture to analyze the extracellular β-glucosidase activity in the culture supernatant). The proteins were separated by ultrafiltration, ammonium sulfate fractionation (40-60%), and High-Q column chromatography, as described previously [15]. The concentrations of protein were analyzed by the Bradford method [26].…”

Section: Enzyme Production and Isolationmentioning

confidence: 99%

See 1 more Smart Citation

Characterization of Three Extracellular ��-Glucosidases Produced by a Fungal Isolate Aspergillus sp. YDJ14 and Their Hydrolyzing Activity for a Flavone Glycoside

Oh¹,

Lee²,

Baek³

et al. 2018

Journal of Microbiology and Biotechnology

Self Cite

View full text Add to dashboard Cite

A cellulolytic fungus, YDJ14, was isolated from compost and identified as an sp. strain. Three extracellular β-glucosidases, BGL-A1, BGL-A2, and BGL-A3, were separated using ultrafiltration, ammonium sulfate fractionation, and High-Q chromatography. The molecular masses of the three enzymes were estimated to be 100, 45, and 40 kDa, respectively, by SDS-PAGE. The optimum pH and temperature of BGL-A3 were 5.0 and 50°C, respectively, whereas the optimum pH and temperature of BGL-A1 and BGL-A2 were identical (4.0 and 60°C, respectively). The half-life of BGL-A3 at 70°C (2.8 min) was shorter than that of BGL-A1 and BGL-A2 (12.1 and 8.8 min, respectively). All three enzymes preferred-nitrophenyl-β--glucopyranoside (NPG) and hardly hydrolyzed cellobiose, suggesting that these enzymes were aryl β-glucosidases. The of BGL-A3 (1.26 mM) forNPG was much higher than that of BGL-A1 and BGL-A2 (0.25 and 0.27 mM, respectively). These results suggested that BGL-A1 and BGL-A2 were similar in their enzymatic properties, whereas BGL-A3 differed from the two enzymes. When tilianin (a flavone glycoside of acacetin) was reacted with the three enzymes, the inhibitory activity for monoamine oxidase, a target in the treatment of neurological disorders, was similar to that shown by acacetin. We conclude that these enzymes may be useful in the hydrolysis of flavone glycosides to improve their inhibitory activities.

show abstract

Characterization of two extracellular β-glucosidases produced from the cellulolytic fungus Aspergillus sp. YDJ216 and their potential applications for the hydrolysis of flavone glycosides

Cited by 21 publications

References 39 publications

Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application

Microbial Beta Glucosidase Enzymes: Recent Advances in Biomass Conversation for Biofuels Application

Characterization of an alkaline esterase from an enriched metagenomic library derived from an oil-spill area

Characterization of Three Extracellular ��-Glucosidases Produced by a Fungal Isolate Aspergillus sp. YDJ14 and Their Hydrolyzing Activity for a Flavone Glycoside

Contact Info

Product

Resources

About