Family 92 carbohydrate-binding modules specific for β-1,6-glucans increase the thermostability of a bacterial chitinase

Li, He; Lu, Zijia; Hao, Mengshu; Kvammen, Alma; Inman, Annie; Srivastava, Vaibhav; Bulone, Vincent; McKee, Lauren S.

doi:10.1016/j.biochi.2023.04.019

Cited by 4 publications

(2 citation statements)

References 54 publications

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“…However, the β-1,6-glucan-binding CBM92 domains characterised in this work are appended to CAZymes with a range of different predicted activities, suggesting that not every member of the family is involved in direct binding to the substrate of an enzyme partner. As β-1,6-glucosidic linkages are found in the cell walls and secretions of marine plants and soil fungi, it may be that tethering, for example, a chitinase 56 or β−1,3-glucanase to a complex cell wall substrate matrix does have a rate-enhancing proximity effect in natural systems 5 .…”

Section: Resultsmentioning

confidence: 99%

Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans

Hao,

Mazurkewich,

et al. 2024

Nat Commun

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Carbohydrate-binding modules (CBMs) are non-catalytic proteins found appended to carbohydrate-active enzymes. Soil and marine bacteria secrete such enzymes to scavenge nutrition, and they often use CBMs to improve reaction rates and retention of released sugars. Here we present a structural and functional analysis of the recently established CBM family 92. All proteins analysed bind preferentially to β−1,6-glucans. This contrasts with the diversity of predicted substrates among the enzymes attached to CBM92 domains. We present crystal structures for two proteins, and confirm by mutagenesis that tryptophan residues permit ligand binding at three distinct functional binding sites on each protein. Multivalent CBM families are uncommon, so the establishment and structural characterisation of CBM92 enriches the classification database and will facilitate functional prediction in future projects. We propose that CBM92 proteins may cross-link polysaccharides in nature, and might have use in novel strategies for enzyme immobilisation.

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Section: Resultsmentioning

confidence: 99%

Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans

Hao,

Mazurkewich,

et al. 2024

Nat Commun

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“…The 2931 cm −1 to 2861 cm −1 peaks designate symmetric and asymmetric stretching of C-H bonds. These bands are polysaccharide-specific and may be detected in the spectra of other polysaccharides such as xylan 103 , glucans 104 , and carrageenans 105 . The bands around 1635 cm −1 and 1590 cm −1 could be accredited to amide groups.…”

Section: Adsorption Mechanismmentioning

confidence: 99%

A combined experimental and modeling approach to elucidate the adsorption mechanism for sustainable water treatment via In2S3-anchored chitosan

Mishra,

Roy,

Gadore

et al. 2023

Sci Rep

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A novel Chitosan/Indium sulfide (CS/In2S3) nanocomposite was created by co-precipitating Chitosan and InCl3 in solution, resulting in In2S3 agglomeration on the Chitosan matrix with a remarkable pore diameter of 170.384 Å, and characterized it for the physical and chemical properties. Under optimal conditions (pH = 7, time = 60 min, catalyst dosage = 0.24 g L−1, and dye concentration = 100 mg L-1), the synthesized nanocomposite demonstrated remarkable adsorption capabilities for Victoria Blue (VB), attaining a removal efficiency of 90.81%. The Sips adsorption isotherm best matched the adsorption process, which followed pseudo-second-order kinetics. With a rate constant of 6.357 × 10–3 g mg−1 min−1, the highest adsorption capacity (qm) was found to be 683.34 mg g−1. Statistical physics modeling (SPM) of the adsorption process revealed multi-interaction and multi-molecular adsorption of VB on the CS/In2S3 surface. The nanocomposite demonstrated improved stability and recyclability, indicating the possibility for low-cost, reusable wastewater dye removal adsorbents. These results have the potential to have practical applications in environmental remediation.

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Enzymatic production of diverse N-acetyl chitooligosaccharides employing a novel bifunctional chitinase and its engineered variants

Liu,

Sun,

Liu

et al. 2024

Food Chemistry

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Family 92 carbohydrate-binding modules specific for β-1,6-glucans increase the thermostability of a bacterial chitinase

Cited by 4 publications

References 54 publications

Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans

Structural and biochemical analysis of family 92 carbohydrate-binding modules uncovers multivalent binding to β-glucans

A combined experimental and modeling approach to elucidate the adsorption mechanism for sustainable water treatment via In2S3-anchored chitosan

Enzymatic production of diverse N-acetyl chitooligosaccharides employing a novel bifunctional chitinase and its engineered variants

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