Plant pathogens as a source of diverse enzymes for lignocellulose digestion

Gibson, Donna M.; King, Brian Christopher; Hayes, Marshall L.; Bergstrom, Gary C.

doi:10.1016/j.mib.2011.04.002

Cited by 110 publications

(73 citation statements)

References 47 publications

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“…However, the dry weight loss was only 8 to 13% over 4 weeks. Recently, there has also been growing interest in the potential of plant-pathogenic fungi to optimize hydrolysis of lignocellulosic biomass (12). For instance, large-scale screening of ascomycetes revealed that the plant pathogens were more active than the nonpathogens on several lignocellulosic substrates (17).…”

Section: Discussionmentioning

confidence: 99%

Exploring the Natural Fungal Biodiversity of Tropical and Temperate Forests toward Improvement of Biomass Conversion

Berrin

Navarro

Couturier

et al. 2012

Appl Environ Microbiol

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fIn this study, natural fungal diversity in wood-decaying species was explored for biomass deconstruction. In 2007 and 2008, fungal isolates were collected in temperate forests mainly from metropolitan France and in tropical forests mainly from French Guiana. We recovered and identified 74 monomorph cultures using morphological and molecular identification tools. Following production of fungal secretomes under inductive conditions, we evaluated the capacity of these fungal strains to potentiate a commercial Trichoderma reesei cellulase cocktail for the release of soluble sugars from biomass. The secretome of 19 isolates led to an improvement in biomass conversion of at least 23%. Of the isolates, the Trametes gibbosa BRFM 952 (Banque de Ressources Fongiques de Marseille) secretome performed best, with 60% improved conversion, a feature that was not universal to the Trametes and related genera. Enzymatic characterization of the T. gibbosa BRFM 952 secretome revealed an unexpected high activity on crystalline cellulose, higher than that of the T. reesei cellulase cocktail. This report highlights the interest in a systematic high-throughput assessment of collected fungal biodiversity to improve the enzymatic conversion of lignocellulosic biomass. It enabled the unbiased identification of new fungal strains issued from biodiversity with high biotechnological potential.

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Section: Discussionmentioning

confidence: 99%

Exploring the Natural Fungal Biodiversity of Tropical and Temperate Forests toward Improvement of Biomass Conversion

Berrin

Navarro

Couturier

et al. 2012

Appl Environ Microbiol

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“…The efficient trans-kingdom transport of bacterial effector proteins is often hindered by the rigid plant cell wall, which mainly consists of cellulose, hemicellulose, and pectin. Bacteria, therefore, often secrete cell wall-degrading enzymes, which contribute to bacterial virulence and include, e.g., cellulases, xylanases, polygalacturonases, and amylases (2)(3)(4)(5)(6). It is assumed that the degradation of plant cell wall components by bacterial enzymes facilitates the acquisition of nutrients as well as the translocation of virulence factors into the host cell (7)(8)(9)(10)(11)(12)(13)(14).…”

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confidence: 99%

Xanthomonas campestris pv. vesicatoria Secretes Proteases and Xylanases via the Xps Type II Secretion System and Outer Membrane Vesicles

et al. 2015

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Many plant-pathogenic bacteria utilize type II secretion (T2S) systems to secrete degradative enzymes into the extracellular milieu. T2S substrates presumably mediate the degradation of plant cell wall components during the host-pathogen interaction and thus promote bacterial virulence. Previously, the Xps-T2S system from Xanthomonas campestris pv. vesicatoria was shown to contribute to extracellular protease activity and the secretion of a virulence-associated xylanase. The identities and functions of additional T2S substrates from X. campestris pv. vesicatoria, however, are still unknown. In the present study, the analysis of 25 candidate proteins from X. campestris pv. vesicatoria led to the identification of two type II secreted predicted xylanases, a putative protease and a lipase which was previously identified as a virulence factor of X. campestris pv. vesicatoria. Studies with mutant strains revealed that the identified xylanases and the protease contribute to virulence and in planta growth of X. campestris pv. vesicatoria. When analyzed in the related pathogen X. campestris pv. campestris, several T2S substrates from X. campestris pv. vesicatoria were secreted independently of the T2S systems, presumably because of differences in the T2S substrate specificities of the two pathogens. Furthermore, in X. campestris pv. vesicatoria T2S mutants, secretion of T2S substrates was not completely absent, suggesting the contribution of additional transport systems to protein secretion. In line with this hypothesis, T2S substrates were detected in outer membrane vesicles, which were frequently observed for X. campestris pv. vesicatoria. We, therefore, propose that extracellular virulence-associated enzymes from X. campestris pv. vesicatoria are targeted to the Xps-T2S system and to outer membrane vesicles. IMPORTANCEThe virulence of plant-pathogenic bacteria often depends on TS2 systems, which secrete degradative enzymes into the extracellular milieu. T2S substrates are being studied in several plant-pathogenic bacteria, including Xanthomonas campestris pv. vesicatoria, which causes bacterial spot disease in tomato and pepper. Here, we show that the T2S system from X. campestris pv. vesicatoria secretes virulence-associated xylanases, a predicted protease, and a lipase. Secretion assays with the related pathogen X. campestris pv. campestris revealed important differences in the T2S substrate specificities of the two pathogens. Furthermore, electron microscopy showed that T2S substrates from X. campestris pv. vesicatoria are targeted to outer membrane vesicles (OMVs). Our results, therefore, suggest that OMVs provide an alternative transport route for type II secreted extracellular enzymes. Many Gram-negative plant-pathogenic bacteria utilize specialized protein secretion systems to deliver virulence factors, including DNA or bacterial effector proteins, into plant cells (1). The efficient trans-kingdom transport of bacterial effector proteins is often hindered by the rigid plant cell wall, which mainly cons...

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“…Microorganisms can produce a wide variety of enzymes that degrade the rigid and complex structure of lignocellulosic materials [11][12][13]8]. In recent years, considerable attention has been focused on the enzymatic degradation of cellulose and hemicellulose as an attractive approach to hydrolyzing lignocellulosic materials [14,15].…”

Section: Asian Journal Of Applied Sciences (Issn: 2321 -0893) Volume mentioning

confidence: 99%

Saccharification of Lignocellulosic Materials by Cellulolytic and Xylanolytic <i>Paenibacillus illioisensis </i>CX11

Ahmed

McKay

2017

AJAS

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The utilization of lignocellulosic materials to produce a variety of building blocks (e.g. fermentable sugars) is an interesting alternative approach to meeting the growing demand for high value chemicals. Cellulose and hemicellulose can be hydrolyzed by cellulase and xylanase enzymes into their respective building blocks (hexoses and pentoses), which can later be converted into the targeted compounds. The aim of this study was to test the ability of Paenibacillus illinoisensis CX11 to saccharify different lignocellulosic materials, and to determine its ability to produce cellulolytic and xylanolytic enzymes for possible use in converting lignocellulosic materials into their respective fermentable sugars. The ability of P. illinoisensis CX11 to produce CMCase, xylanase, FPase, and avicelase was tested using SSF of corn stalk. Furthermore, the ability of P. illinoisensis CX11 to saccharify lignocellulosic materials was tested using corn stalk, wheat bran, sawdust, and corn cob. The amount of reducing sugars released from the saccharification of lignocellulosic materials was determined by the 3,5-dinitro-salicylic acid (DNS) method. Obtained results showed that P. illinoisensis CX11 can produce CMCase (400.12 Â± 1.23 U/L), xylanase (385.57 Â± 2.25 U/L), FPase (266.93 Â± 2.22 U/L), avicelase (187.85 Â± 2.22 U/L) and extracellular protein (4.56 Â± 0.14 mg/L). Moreover, P. illinoisensis CX11 showed an ability to saccharify lignocellulosic materials. These findings confirm that P. illinoisensis CX11 has the ability to produce cellulolytic and xylanolytic enzymes, and to hydrolyze different lignocellulosic materials into fermentable sugars. Therefore, this study concludes that P. illinoisensis CX11 can be considered a good source of cellulase and xylanase enzymes to saccharify different lignocellulosic materials.

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Plant pathogens as a source of diverse enzymes for lignocellulose digestion

Cited by 110 publications

References 47 publications

Exploring the Natural Fungal Biodiversity of Tropical and Temperate Forests toward Improvement of Biomass Conversion

Exploring the Natural Fungal Biodiversity of Tropical and Temperate Forests toward Improvement of Biomass Conversion

Xanthomonas campestris pv. vesicatoria Secretes Proteases and Xylanases via the Xps Type II Secretion System and Outer Membrane Vesicles

Saccharification of Lignocellulosic Materials by Cellulolytic and Xylanolytic <i>Paenibacillus illioisensis </i>CX11

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