A rationally identified marine <scp>GH1</scp> β‐glucosidase has distinguishing functional features for simultaneous saccharification and fermentation

Sousa, Amanda Silva de; Melo, Ricardo Rodrigues de; Miyamoto, Renan Yuji; Morais, M.A.B.; Andrade, Liliane Pires; Milan, N; Ávila, Mayara Chagas de; Souza, Cláudia M. de; Adão, Regina; Scarpassa, Josiane Aniele; Vieira, P.S.; Santos, Leandro Vieira dos; Ramos, Carlos Henrique Inácio; Murakami, Mário Tyago; Zanphorlin, L.M.

doi:10.1002/bbb.2136

Cited by 6 publications

(4 citation statements)

References 72 publications

(151 reference statements)

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“…Size-exclusion chromatography coupled with multi-angle light scattering (SEC-MALS) experiments were performed at 25 °C using a triple-angle static light scattering detector miniDAWN™ TREOS and Optilab ® T-rEX refractive index monitor (Wyatt Technology) coupled to an ÄKTA fast protein liquid chromatography system (GE Healthcare) with a Superdex 200 HR 10/300 GL analytical size-exclusion column (GE Healthcare) 62 . 250 μL from purified wild-type Xac GalD and mutant S106R at 50 μmol L −1 were injected separately into the column and eluted in 20 mmol L −1 HEPES pH 7.5, 150 mmol L −1 NaCl.…”

Section: Methodsmentioning

confidence: 99%

Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors

et al. 2021

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Xyloglucans are highly substituted and recalcitrant polysaccharides found in the primary cell walls of vascular plants, acting as a barrier against pathogens. Here, we reveal that the diverse and economically relevant Xanthomonas bacteria are endowed with a xyloglucan depolymerization machinery that is linked to pathogenesis. Using the citrus canker pathogen as a model organism, we show that this system encompasses distinctive glycoside hydrolases, a modular xyloglucan acetylesterase and specific membrane transporters, demonstrating that plant-associated bacteria employ distinct molecular strategies from commensal gut bacteria to cope with xyloglucans. Notably, the sugars released by this system elicit the expression of several key virulence factors, including the type III secretion system, a membrane-embedded apparatus to deliver effector proteins into the host cells. Together, these findings shed light on the molecular mechanisms underpinning the intricate enzymatic machinery of Xanthomonas to depolymerize xyloglucans and uncover a role for this system in signaling pathways driving pathogenesis.

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Section: Methodsmentioning

confidence: 99%

Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors

et al. 2021

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“…Higher substrate affinity with BGL may be due to the F256 binding residue that is located on a shorter loop [ 79 ]. The Exiguobacterium marinum BGL was found to be able to process longer cello-oligosaccharides, which is atypical in the GH1 family, and the discovery of this structure at the topologically specific catalytic interface provides a theoretical basis for designing BGLs with a strong capacity for cleaving cellulose oligosaccharides [ 80 ].…”

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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“…The higher substrate affinity with BGL may be that the F256 binding residue is located on a shorter loop [77]. The Exiguobacterium marinum BGL was found to be able to process longer cello-oligosaccharides, which is atypical in the GH1 family, and the discovery of this structure at the topologically specific catalytic interface provides a theoretical basis for designing BGLs with strong capacity of cleaving cellulose oligosaccharides [78].…”

Section: Enhancing Activitymentioning

confidence: 99%

Recent Advances in β-glucosidase Engineering: A Brief Review

Zhao¹,

Huang²,

Ouyang³

et al. 2023

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A rationally identified marine GH1 β‐glucosidase has distinguishing functional features for simultaneous saccharification and fermentation

Cited by 6 publications

References 72 publications

Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors

Xyloglucan processing machinery in Xanthomonas pathogens and its role in the transcriptional activation of virulence factors

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

Recent Advances in β-glucosidase Engineering: A Brief Review

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