Carbohydrate binding modules enhance cellulose enzymatic hydrolysis by increasing access of cellulases to the substrate

Bernardes, Amanda; Pellegrini, Vanessa de Oliveira Arnoldi; Curtolo, Felipe; Camilo, César M.; Mello, Bruno Luan; Johns, Marcus A.; Scott, Janet L.; Guimarães, Francisco; Polikarpov, Igor

doi:10.1016/j.carbpol.2019.01.108

Cited by 91 publications

(49 citation statements)

References 58 publications

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“…activity, but does help in binding GHs to polysaccharides, strengthening their activity (Du et al, 2018;Bernardes et al, 2019). Levels of CBMs in the withering period were significantly higher than in the other two periods.…”

Section: Adaption Strategies Of Rumen Microorganisms In Tibetan Sheepmentioning

confidence: 98%

Tibetan Sheep Adapt to Plant Phenology in Alpine Meadows by Changing Rumen Microbial Community Structure and Function

Liu

Han

et al. 2020

Front. Microbiol.

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The rumen microbiota is strongly associated with host health, nutrient absorption, and adaptability. However, the composition, functioning and adaptability of rumen microbiota in Tibetan sheep (TS) across different phenological periods are unclear. In this study we used sequencing of the V4-V5 region of 16S rRNA, qPCR technology and metagenomics to investigate the adaption of rumen microbiota to forage in different stages of phenology. In a grassy period, due to the high nutritional quality of the forage, TS can produce high concentrations of NH 3-N and short fatty acids by increasing the content of key bacteria in the rumen, such as Bacteroidetes, Prevotella, Succiniclasticum, Treponema, Butyrivibrio fibrisolvens, Fibrobacter succinogenes, Prevotella ruminicola, Ruminococcus albus, and Ruminococcus flavefaciens to aid in growth. In the withering period, there was a positive correlation between microorganisms which indicated the closely cooperation between microorganisms, and metagenomic analysis showed that the high genes (GHs and CBMs) and subtribe (GH8,

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Section: Adaption Strategies Of Rumen Microorganisms In Tibetan Sheepmentioning

confidence: 98%

Tibetan Sheep Adapt to Plant Phenology in Alpine Meadows by Changing Rumen Microbial Community Structure and Function

Liu

Han

et al. 2020

Front. Microbiol.

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“…CBMs do not have catalytic activity but function as substrate binding modules (Boraston et al, 2004;Lombard et al, 2014). It has been suggested that the binding characteristic of a CBM improves catalytic function of the CAZymes through targeting the enzyme to the substrate and increasing substrate-enzyme proximity as well as disrupting the crystallinity of the insoluble substrate fraction (Arantes and Saddler, 2010;Reyes-Ortiz et al, 2013;Bernardes et al, 2019;Chalak et al, 2019). As a consequence, the removal of the CBM from the enzyme results in a decreased enzymatic activity (Arai et al, 2003;Cockburn et al, 2017) and a reduced enzyme stability (Bissaro et al, 2017;Courtade et al, 2018;Teo et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms

Sidar

Albuquerque²,

Voshol³

et al. 2020

Front. Bioeng. Biotechnol.

105

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Enzymatic degradation of abundant renewable polysaccharides such as cellulose and starch is a field that has the attention of both the industrial and scientific community. Most of the polysaccharide degrading enzymes are classified into several glycoside hydrolase families. They are often organized in a modular manner which includes a catalytic domain connected to one or more carbohydrate-binding modules. The carbohydrate-binding modules (CBM) have been shown to increase the proximity of the enzyme to its substrate, especially for insoluble substrates. Therefore, these modules are considered to enhance enzymatic hydrolysis. These properties have played an important role in many biotechnological applications with the aim to improve the efficiency of polysaccharide degradation. The domain organization of glycoside hydrolases (GHs) equipped with one or more CBM does vary within organisms. This review comprehensively highlights the presence of CBM as ancillary modules and explores the diversity of GHs carrying one or more of these modules that actively act either on cellulose or starch. Special emphasis is given to the cellulase and amylase distribution within the filamentous microorganisms from the genera of Streptomyces and Aspergillus that are well known to have a great capacity for secreting a wide range of these polysaccharide degrading enzyme. The potential of the CBM and other ancillary domains for the design of improved polysaccharide decomposing enzymes is discussed.

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“…CBMs not only target the enzymes to their substrates to promote catalysis [30, 31], but sometimes they can also modulate enzyme specificity [32]. CBMs are devoid of catalytic activity, but some studies suggest they play a role in the amorphization of cellulose through non-hydrolytic disruption of the crystalline structure of cellulose [33, 34]. CBM1 appended to AA9 LPMOs may influence substrate binding, enzyme activity and/or regioselectivity, but the data are scarce and reported observations are contradictory.…”

Section: Introductionmentioning

confidence: 99%

Influence of the carbohydrate-binding module on the activity of a fungal AA9 lytic polysaccharide monooxygenase on cellulosic substrates

Chalak

Villares

Moreau

et al. 2019

Biotechnol Biofuels

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Background: Cellulose-active lytic polysaccharide monooxygenases (LPMOs) secreted by filamentous fungi play a key role in the degradation of recalcitrant lignocellulosic biomass. They can occur as multidomain proteins fused to a carbohydrate-binding module (CBM). From a biotech perspective, LPMOs are promising innovative tools for producing nanocelluloses and biofuels, but their direct action on cellulosic substrates is not fully understood. Results:In this study, we probed the role of the CBM from family 1 (CBM1) appended to the LPMO9H from Podospora anserina (PaLPMO9H) using model cellulosic substrates. Deletion of the CBM1 weakened the binding to cellulose nanofibrils, amorphous and crystalline cellulose. Although the release of soluble sugars from cellulose was drastically reduced under standard conditions, the truncated LPMO retained some activity on soluble oligosaccharides. The cellulolytic action of the truncated LPMO was demonstrated using synergy experiments with a cellobiohydrolase (CBH). The truncated LPMO was still able to improve the efficiency of the CBH on cellulose nanofibrils in the same range as the full-length LPMO. Increasing the substrate concentration enhanced the performance of PaLPMO9H without CBM in terms of product release. Interestingly, removing the CBM also altered the regioselectivity of PaLPMO9H, significantly increasing cleavage at the C1 position. Analysis of the insoluble fraction of cellulosic substrates evaluated by optical and atomic force microscopy confirmed that the CBM1 module was not strictly required to promote disruption of the cellulose network. Conclusions:Absence of the CBM1 does not preclude the activity of the LPMO on cellulose but its presence has an important role in driving the enzyme to the substrate and releasing more soluble sugars (both oxidized and nonoxidized), thus facilitating the detection of LPMO activity at low substrate concentration. These results provide insights into the mechanism of action of fungal LPMOs on cellulose to produce nanocelluloses and biofuels.

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Carbohydrate binding modules enhance cellulose enzymatic hydrolysis by increasing access of cellulases to the substrate

Cited by 91 publications

References 58 publications

Tibetan Sheep Adapt to Plant Phenology in Alpine Meadows by Changing Rumen Microbial Community Structure and Function

Tibetan Sheep Adapt to Plant Phenology in Alpine Meadows by Changing Rumen Microbial Community Structure and Function

Carbohydrate Binding Modules: Diversity of Domain Architecture in Amylases and Cellulases From Filamentous Microorganisms

Influence of the carbohydrate-binding module on the activity of a fungal AA9 lytic polysaccharide monooxygenase on cellulosic substrates

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