Characterization of a glucose-stimulated β-glucosidase from Microbulbifer sp. ALW1

Jiang, Zhen; Long, Liufei; Liang, Meifang; Li, Hebin; Chen, Yanhong; Zheng, Mingjing; Ni, Hui; Li, Qingbiao; Zhu, Yanbing

doi:10.1016/j.micres.2021.126840

Cited by 17 publications

(10 citation statements)

References 49 publications

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“…which exhibited a t 1/2 of 20 min at 40 °C [ 30 ], and Microbulbifer sp. ALW1 BGL which showed less than 20% of the original activity after 120 min at a temperature between 40 and 45 °C [ 31 ].…”

Section: Resultsmentioning

confidence: 99%

“…The inhibitory effect of SDS was previously reported on BGL from A. f lavus [ 28 ], Microbulbifer sp. ALW1 [ 31 ], and Penicillium roqueforti [ 35 ]. The negative effects of SDS on enzyme activity have been ascribed to the detergent's interference with the enzymes' hydrophobic regions as well as the tertiary structure, leading to denaturation [ 20 ].…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

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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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

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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“…Some GH enzymes from Microbulbifer sp. ALW1 have been characterised in our previous work, including a novel laminarinase MaLamNA (Hu et al 2021 ), a β-glucosidase MaGlu1A belonging to GH1 (Jiang et al 2021 ), and an endo-β-1,4-glucanase MaCel5A belonging to GH5 (Li et al 2021a ). Polysaccharide lyases have substrate specificity and can break the O–C4 bond to the uronic acid using a β-elimination mechanism (Li et al 2021b ).…”

Section: Discussionmentioning

confidence: 99%

Characterisation of marine bacterium Microbulbifer sp. ALW1 with Laminaria japonica degradation capability

Li³

et al. 2022

AMB Expr

Self Cite

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Marine bacterium Microbulbifer sp. ALW1 was revealed to be able to effectively degrade Laminaria japonica thallus fragments into fine particles. Polysaccharide substrate specificity analysis indicated that ALW1 could produce extracellular alginate lyase, laminarinase, fucoidanase and cellulase. Based on alignment of the 16 S rRNA sequence with other reference relatives, ALW1 showed the closest relationship with Microbulbifer aggregans CCB-MM1T. The cell morphology and some basic physiological and biochemical parameters of ALW1 cells were characterised. ALW1 is a Gram-negative, rod- or oval-shaped, non-spore-forming and non-motile bacterium. The DNA–DNA relatedness values of ALW1 with type strains of M. gwangyangensis (JCM 17,800), M. aggregans (JCM 31,875), M. maritimus (JCM 12,187), M. okinawensis (JCM 16,147) and M. rhizosphaerae (DSM 28,920) were 28.9%, 43.3%, 41.2%, 35.4% and 45.6%, respectively. The major cell wall sugars of ALW1 were determined to be ribose and galactose, which differed from other closely related species. These characteristics indicated that ALW1 could be assigned to a separate species of the genus Microbulbifer. The complete genome of ALW1 contained one circular chromosome with 4,682,287 bp and a GC content of 56.86%. The putative encoded proteins were categorised based on their functional annotations. Phenotypic, physiological, biochemical and genomic characterisation will provide insights into the many potential industrial applications of Microbulbifer sp. ALW1.Key points.

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“…Based on this property, the molecular mechanism of BGL product tolerance suggests that increasing the hydrophobicity of the aglycone-binding sites (+1 and +2 subsites) in the active site tunnel and the hydrophobicity and steric properties of the non-conserved residues in the gatekeeper region can improve BGL product tolerance. Other inactive sites are also associated with high tolerance of BGL products, including separate glucose binding sites [ 85 ] and some active channel residues [ 86 ]. Table 3 summarizes examples for enhancing product tolerance of BGLs in recent years.…”

Section: Engineering Of Bgl Functionalitiesmentioning

confidence: 99%

Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review

et al. 2023

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β-glucosidases (BGLs) play a crucial role in the degradation of lignocellulosic biomass as well as in industrial applications such as pharmaceuticals, foods, and flavors. However, the application of BGLs has been largely hindered by issues such as low enzyme activity, product inhibition, low stability, etc. Many approaches have been developed to engineer BGLs to improve these enzymatic characteristics to facilitate industrial production. In this article, we review the recent advances in BGL engineering in the field, including the efforts from our laboratory. We summarize and discuss the BGL engineering studies according to the targeted functions as well as the specific strategies used for BGL engineering.

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Characterization of a glucose-stimulated β-glucosidase from Microbulbifer sp. ALW1

Cited by 17 publications

References 49 publications

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

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

Characterisation of marine bacterium Microbulbifer sp. ALW1 with Laminaria japonica degradation capability

Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review

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