A new and unusual β-glucosidase from Aspergillus fumigatus: Catalytic activity at high temperatures and glucose tolerance

Ratuchne, Aline; Knob, Adriana

doi:10.1016/j.bcab.2021.102064

Cited by 9 publications

(2 citation statements)

References 34 publications

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“…This enzyme can be efficiently synthesized using an economical culture medium, such as canola meal, as a substrate. Remarkably, the enzyme exhibited a significant activity level, achieving 24.53 U/mL, when cultivated with 2.9% canola flour at a pH of 4.2 over 101 h at a temperature of 40 °C [ 46 ].…”

Section: Upstream Bioprocessingmentioning

confidence: 99%

Upstream and Downstream Bioprocessing in Enzyme Technology

Guajardo,

Schrebler

2023

Pharmaceutics

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The development of biotransformation must integrate upstream and downstream processes. Upstream bioprocessing will influence downstream bioprocessing. It is essential to consider this because downstream processes can constitute the highest cost in bioprocessing. This review comprehensively overviews the most critical aspects of upstream and downstream bioprocessing in enzymatic biocatalysis. The main upstream processes discussed are enzyme production, enzyme immobilization methodologies, solvent selection, and statistical optimization methodologies. The main downstream processes reviewed in this work are biocatalyst recovery and product separation and purification. The correct selection and combination of upstream and downstream methodologies will allow the development of a sustainable and highly productive system.

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Section: Upstream Bioprocessingmentioning

confidence: 99%

Upstream and Downstream Bioprocessing in Enzyme Technology

Guajardo,

Schrebler

2023

Pharmaceutics

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“…As a result, the quest for high-glucose-tolerant β-glucosidases has gained prominence ( de Giuseppe et al, 2014 ). Elevated temperature conditions offer manifold advantages, including augmented enzyme-substrate interaction rates, reduced contamination risks, heightened matrix solubility, and accelerated diffusion rates ( Schröder et al, 2014 ; Ratuchne and Knob, 2021 ). Consequently, numerous industrial processes are conducted under high-temperature conditions.…”

Section: Introductionmentioning

confidence: 99%

Characterization of a thermophilic and glucose-tolerant GH1 β-glucosidase from hot springs and its prospective application in corn stover degradation

Huang,

Lv,

Zheng

et al. 2023

Front. Microbiol.

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Introductionβ-Glucosidase serves as the pivotal rate-limiting enzyme in the cellulose degradation process, facilitating the hydrolysis of cellobiose and cellooligosaccharides into glucose. However, the widespread application of numerous β-glucosidases is hindered by their limited thermostability and low glucose tolerance, particularly in elevated-temperature and high-glucose environments.MethodsThis study presents an analysis of a β-glucosidase gene belonging to the GH1 family, denoted lqbg8, which was isolated from the metagenomic repository of Hehua hot spring located in Tengchong, China. Subsequently, the gene was cloned and heterologously expressed in Escherichia coli BL21(DE3). Post expression, the recombinant β-glucosidase (LQBG8) underwent purification through a Ni affinity chromatography column, thereby enabling the in-depth exploration of its enzymatic properties.ResultsLQBG8 had an optimal temperature of 70°C and an optimum pH of 5.6. LQBG8 retained 100 and 70% of its maximum activity after 2-h incubation periods at 65°C and 70°C, respectively. Moreover, even following exposure to pH ranges of 3.0–10.0 for 24 h, LQBG8 retained approximately 80% of its initial activity. Notably, the enzymatic prowess of LQBG8 remained substantial at glucose concentrations of up to 3 M, with a retention of over 60% relative activity. The kinetic parameters of LQBG8 were characterized using cellobiose as substrate, with Km and Vmax values of 28 ± 1.9 mg/mL and 55 ± 3.2 μmol/min/mg, respectively. Furthermore, the introduction of LQBG8 (at a concentration of 0.03 mg/mL) into a conventional cellulase reaction system led to an impressive 43.7% augmentation in glucose yield from corn stover over a 24-h period. Molecular dynamics simulations offered valuable insights into LQBG8’s thermophilic nature, attributing its robust stability to reduced fluctuations, conformational changes, and heightened structural rigidity in comparison to mesophilic β-glucosidases.DiscussionIn summation, its thermophilic, thermostable, and glucose-tolerant attributes, render LQBG8 ripe for potential applications across diverse domains encompassing food, feed, and the production of lignocellulosic ethanol.

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Inactivation and process intensification of β-glucosidase in biomass utilization

Meng

et al. 2023

Appl Microbiol Biotechnol

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A new and unusual β-glucosidase from Aspergillus fumigatus: Catalytic activity at high temperatures and glucose tolerance

Cited by 9 publications

References 34 publications

Upstream and Downstream Bioprocessing in Enzyme Technology

Upstream and Downstream Bioprocessing in Enzyme Technology

Characterization of a thermophilic and glucose-tolerant GH1 β-glucosidase from hot springs and its prospective application in corn stover degradation

Inactivation and process intensification of β-glucosidase in biomass utilization

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