Cloning, expression, biochemical characterization, and molecular docking studies of a novel glucose tolerant β-glucosidase from Saccharomonospora sp. NB11

Zada, Numan Saleh; Beldüz, Ali Osman; Güler, Halil İbrahim; Khan, Anum; Sahinkaya, Miray; Kaçıran, Arife; Ay, Hilal; Badshah, Malik; Shah, Aamer Ali; Khan, Samiullah

doi:10.1016/j.enzmictec.2021.109799

Cited by 12 publications

(4 citation statements)

References 39 publications

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“…To our surprise, purified recombinant AoBgl hydrolysed only p-NPG but, there was no detectable cellobiose hydrolysing activity for this enzyme. We would like to emphasise that this as an important observation as several published literature characterized β-glucosidases based on p-NPG hydrolysis activity only (42)(43)(44)(45). Our study shows that p-NPG hydrolysis cannot be considered to mimic enzymatic hydrolysis activity on real disaccharide substrates like cellobiose.…”

Section: Discussionmentioning

confidence: 81%

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Molecular insights into the oligosaccharide binding, recognition and hydrolysis by a fungal exo-β-(1,3)-glucanase

Banerjee,

Kamale,

Suryawanshi

et al. 2024

Preprint

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Carbohydrate hydrolysing enzymes assume special industrial and commercial interest as a source for yielding fermentable glucose especially for the biofuel industry. Among these enzymes, the exo-β-(1,3) glucanases are promising for industrial use as they hydrolyze sugars such as laminarin, a major constituent of the algal cell wall. Exploring the structure and function of these enzymes is of particular interest for the improvement of their functional properties for industrial use. We report the structural and biochemical characterizations ofAspergillus oryzaeexo-β-(1,3) glucanase (AoBgl). We have expressed, purified, and performed biochemical characterizations of the recombinant AoBgl. Purified AoBgl is found to hydrolyse β-(1,3)-glycosidic linkages present in the oligosaccharide laminaritriose and the polysaccharide, laminarin effectively while retaining >50% activity at glucose concentrations of around 1.5M. We have determined three high-resolution structures of AoBgl: (a) apo form at 1.75 Å, (b) complexed form with bound disaccharide at 1.73 Å and (c) glucose-bound form at 1.20 Å. Sequence analysis and structural comparison indicate that AoBgl belongs to the GH5 sugar hydrolase family. The sugar-bound structures reveal the mode of substrate binding and interactions at the active site of AoBgl. Further, molecular dynamics simulation and mutational studies indicate that AoBgl can effectively bind trisaccharides and higher oligosaccharides. Our biochemical and structural data provide detailed molecular insights into the active site of this GH5 enzyme and would be helpful in the rational engineering of glycosyl hydrolases belonging to similar families for industrial use.

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Section: Discussionmentioning

confidence: 81%

“…Several glycosyl hydrolases with conserved overall structural fold (30,34,41,42,46,47) might hydrolyse p-NPG; however, hydrolysis of the actual substrate might require proper positioning of the catalytic motifs for the activity. The inability hydrolyse cellobiose confirms that AoBgl is not a β-glucosidase that can act on β- (1,4) linkages.…”

Section: Discussionmentioning

confidence: 99%

Molecular insights into the oligosaccharide binding, recognition and hydrolysis by a fungal exo-β-(1,3)-glucanase

Banerjee,

Kamale,

Suryawanshi

et al. 2024

Preprint

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“…All other docking parameters were set to default. Subsequently, the most suitable BGL-ligand pose was chosen and visualised using PyMol [ 23 ].…”

Section: Methodsmentioning

confidence: 99%

Biochemical and in silico structural properties of a thermo-acid stable β-glucosidase from Beauveria bassiana

Magwaza,

Amobonye,

Bhagwat

et al. 2024

Heliyon

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“…The Lb0241 gene was cloned using the method of Saleh Zada et al (2021) with slight modifications. The gene encoding Lb0241 was amplified from L. brevis T61 genomic DNA.…”

Section: Methodsmentioning

confidence: 99%

Cloning and expression of Lactobacillus brevis β‐glucosidase and its effect on the aroma of strawberry wine

Xia

Wang

et al. 2022

Food Processing Preservation

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Aroma is one of the key characteristics of fruit wine and is correlated to volatile organic compounds, which greatly influences the purchase intention of consumers (Zhang, Wang, et al., 2021). Although the major aroma compounds, mainly derived from the fruit, are produced during the alcoholic fermentation stage, a number of odorless non-volatile glycosides are also present, which are often considered as aroma precursors; the hydrolysis of these glycosides could significantly improve the natural aroma compounds of fruit wine (Aaby et al., 2018;Michlmayr et al., 2010). Therefore, researchers have attempted to develop effective methods to hydrolyze these nonvolatile glycosides to release the free aroma compounds (Michlmayr et al., 2010). Lactic acid bacteria (LAB) can hydrolyze glycosylated

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Cloning, expression, biochemical characterization, and molecular docking studies of a novel glucose tolerant β-glucosidase from Saccharomonospora sp. NB11

Cited by 12 publications

References 39 publications

Molecular insights into the oligosaccharide binding, recognition and hydrolysis by a fungal exo-β-(1,3)-glucanase

Molecular insights into the oligosaccharide binding, recognition and hydrolysis by a fungal exo-β-(1,3)-glucanase

Biochemical and in silico structural properties of a thermo-acid stable β-glucosidase from Beauveria bassiana

Cloning and expression of Lactobacillus brevis β‐glucosidase and its effect on the aroma of strawberry wine

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