Unconventional β-Glucosidases: A Promising Biocatalyst for Industrial Biotechnology

Godse, Ravish; Bawane, Hemangi; Tripathi, Jyoti; Kulkarni, Ram

doi:10.1007/s12010-021-03568-y

Cited by 26 publications

(9 citation statements)

References 122 publications

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“…We found five conserved motifs that also included the conserved TENG and NEPX motifs of β-glucosidases. The results of multiple sequence alignment revealed that E192 and E393 are highly substrates, these enzymes exist widely in nature and exhibit a range of functions (Godse et al, 2021). Studies have shown that β-glucosidase promotes the formation of free terpenes, phenylpropenes, and specific aliphatic esters during wine fermentation and promotes the production of wine aroma compounds that affect the aroma and flavor of the product (Liu et al, 2021).…”

Section: Discussionmentioning

confidence: 99%

“…β-glucosidases primarily catalyze the removal of terminal non-reducing β-D-glucosyl residues from various glucoconjugates, including glucosides, oligosaccharides, and 1-O-glucosyl esters, as well as perform transglycosylation and reverse hydrolysis. Due to the extensive distribution of their substrates, these enzymes exist widely in nature and exhibit a range of functions ( Godse et al, 2021 ). Studies have shown that β-glucosidase promotes the formation of free terpenes, phenylpropenes, and specific aliphatic esters during wine fermentation and promotes the production of wine aroma compounds that affect the aroma and flavor of the product ( Liu et al, 2021 ).…”

Section: Discussionmentioning

confidence: 99%

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Molecular Cloning and Functional Characterization of a β-Glucosidase Gene to Produce Platycodin D in Platycodon grandiflorus

Meng

Liu

et al. 2022

Front. Plant Sci.

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Platycodin D (PD) is a deglycosylated triterpene saponin with much higher pharmacological activity than glycosylated platycoside E (PE). Extensive studies in vitro showed that the transformation of platycoside E to platycodin D can be achieved using β-glucosidase extracted from several bacteria. However, whether similar enzymes in Platycodon grandiflorus could convert platycoside E to platycodin D, as well as the molecular mechanism underlying the deglycosylation process of platycodon E, remain unclear. Here, we identified a β-glucosidase in P. grandiflorus from our previous RNA-seq analysis, with a full-length cDNA of 1,488 bp encoding 495 amino acids. Bioinformatics and phylogenetic analyses showed that β-glucosidases in P. grandiflorus have high homology with other plant β-glucosidases. Subcellular localization showed that there is no subcellular preference for its encoding gene. β-glucosidase was successfully expressed as 6 × His-tagged fusion protein in Escherichia coli BL21 (DE3). Western blot analysis yielded a recombinant protein of approximately 68 kDa. In vitro enzymatic reactions determined that β-glucosidase was functional and could convert PE to PD. RT-qPCR analysis showed that the expression level of β-glucosidase was higher at night than during the day, with the highest expression level between 9:00 and 12:00 at night. Analysis of the promoter sequence showed many light-responsive cis-acting elements, suggesting that the light might regulate the gene. The results will contribute to the further study of the biosynthesis and metabolism regulation of triterpenoid saponins in P. grandiflorus.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Molecular Cloning and Functional Characterization of a β-Glucosidase Gene to Produce Platycodin D in Platycodon grandiflorus

Meng

Liu

et al. 2022

Front. Plant Sci.

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“…β-glucosidase is a critical enzyme for complete hydrolysis of cellulosic biomass as it produces glucose from oligosaccharides and cellobiose. The stability of this enzyme toward operational conditions is a critical parameter in industrial settings [134,135]. The 3 h incubation of the bulk crude enzyme with 75 mM of H 2 O 2 showed 1.34-fold enhancements in BGL activity, suggesting a high tolerance with potential application in oxidative pretreatment conditions.…”

Section: Discussionmentioning

confidence: 99%

A Lignocellulolytic Colletotrichum sp. OH with Broad-Spectrum Tolerance to Lignocellulosic Pretreatment Compounds and Derivatives and the Efficiency to Produce Hydrogen Peroxide and 5-Hydroxymethylfurfural Tolerant Cellulases

Chanda

Mozumder

Chorei

et al. 2021

JoF

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Fungal endophytes are an emerging source of novel traits and biomolecules suitable for lignocellulosic biomass treatment. This work documents the toxicity tolerance of Colletotrichum sp. OH toward various lignocellulosic pretreatment-derived inhibitors. The effects of aldehydes (vanillin, p-hydroxybenzaldehyde, furfural, 5-hydroxymethylfurfural; HMF), acids (gallic, formic, levulinic, and p-hydroxybenzoic acid), phenolics (hydroquinone, p-coumaric acid), and two pretreatment chemicals (hydrogen peroxide and ionic liquid), on the mycelium growth, biomass accumulation, and lignocellulolytic enzyme activities, were tested. The reported Colletotrichum sp. OH was naturally tolerant to high concentrations of single inhibitors like HMF (IC50; 17.5 mM), levulinic acid (IC50; 29.7 mM), hydroquinone (IC50; 10.76 mM), and H2O2 (IC50; 50 mM). The lignocellulolytic enzymes displayed a wide range of single and mixed inhibitor tolerance profiles. The enzymes β-glucosidase and endoglucanase showed H2O2- and HMF-dependent activity enhancements. The enzyme β-glucosidase activity was 34% higher in 75 mM and retained 20% activity in 125 mM H2O2. Further, β-glucosidase activity increased to 24 and 32% in the presence of 17.76 and 8.8 mM HMF. This research suggests that the Colletotrichum sp. OH, or its enzymes, can be used to pretreat plant biomass, hydrolyze it, and remove inhibitory by-products.

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“…Trichoderma reesei is one of the most extensively used fungal species to produce cellulolytic enzymes in industry, due to its extraordinary high secretion capacity for enzymes, especially efficient cellulases [16,24,47,61,62]. Still, it lacks sufficient β-glucosidase activity for efficient cellulose hydrolysis and there are numerous examples on supplementation of cellulases from T. reesei with β-glucosidase preparations, especially from Aspergillus niger or other Aspergillus species [4,37,[63][64][65][66]. However, industrial production of cellobiohydrolases and β-glucosidases in separate organisms is expensive because of the requirement for double equipment.…”

Section: Production Of Enzymes For Plant Biomass Utilizationmentioning

confidence: 99%

Fungal Cell Factories for Efficient and Sustainable Production of Proteins and Peptides

Lübeck

2022

Microorganisms

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Filamentous fungi are a large and diverse taxonomically group of microorganisms found in all habitats worldwide. They grow as a network of cells called hyphae. Since filamentous fungi live in very diverse habitats, they produce different enzymes to degrade material for their living, for example hydrolytic enzymes to degrade various kinds of biomasses. Moreover, they produce defense proteins (antimicrobial peptides) and proteins for attaching surfaces (hydrophobins). Many of them are easy to cultivate in different known setups (submerged fermentation and solid-state fermentation) and their secretion of proteins and enzymes are often much larger than what is seen from yeast and bacteria. Therefore, filamentous fungi are in many industries the preferred production hosts of different proteins and enzymes. Edible fungi have traditionally been used as food, such as mushrooms or in fermented foods. New trends are to use edible fungi to produce myco-protein enriched foods. This review gives an overview of the different kinds of proteins, enzymes, and peptides produced by the most well-known fungi used as cell factories for different purposes and applications. Moreover, we describe some of the challenges that are important to consider when filamentous fungi are optimized as efficient cell factories.

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Unconventional β-Glucosidases: A Promising Biocatalyst for Industrial Biotechnology

Cited by 26 publications

References 122 publications

Molecular Cloning and Functional Characterization of a β-Glucosidase Gene to Produce Platycodin D in Platycodon grandiflorus

Molecular Cloning and Functional Characterization of a β-Glucosidase Gene to Produce Platycodin D in Platycodon grandiflorus

A Lignocellulolytic Colletotrichum sp. OH with Broad-Spectrum Tolerance to Lignocellulosic Pretreatment Compounds and Derivatives and the Efficiency to Produce Hydrogen Peroxide and 5-Hydroxymethylfurfural Tolerant Cellulases

Fungal Cell Factories for Efficient and Sustainable Production of Proteins and Peptides

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