High-Level Expression and Efficient Purification of Bioactive Swollenin in Aspergillus oryzae

Wang, Meihua; Cai, Jin; Huang, Lei; Lv, Zhengbin; Zhang, Yaozhou; Xu, Zhinan

doi:10.1007/s12010-010-8978-0

Cited by 23 publications

(17 citation statements)

References 20 publications

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“…In literature, experimental evidences concerning the synergism between expansin-like proteins and cellulases exist (Chen et al 2010;Kim et al 2009;Lee et al 2010;QuirozCastañeda et al 2011;Wang et al 2010Wang et al , 2011Zhou et al 2011). In all these studies, BSA was used as a nonspecific control protein.…”

Section: Discussionmentioning

confidence: 99%

“…Combined action on filter paper by CP and cellulase As expansin-like proteins can enhance the yield of reducing sugars produced by hydrolytic enzymes when applied together on cellulosic materials (Chen et al 2010;Kim et al 2009;Lee et al 2010;Quiroz-Castañeda et al 2011;Wang et al 2010Wang et al , 2011Zhou et al 2011), accordingly the synergistic effect of CP and cellulases was tested in the present study.…”

Section: Binding To Polysaccharidesmentioning

confidence: 99%

“…to increase the efficiency of bioconversion of lignocellulose to ethanol (Arantes and Saddler 2010;Jäger et al 2011). These objectives are supported by a number of experimental data concerning the synergism with cellulases (Chen et al 2010;Kim et al 2009;Lee et al 2010;Quiroz-Castañeda et al 2011;Wang et al 2010Wang et al , 2011Zhou et al 2011). However, the biological role of expansin-type protein domains from microbes seems that of facilitating the interaction with plants, as colonization or symbiosis establishment (Brotman et al 2008;Dermatsev et al 2010;Kerff et al 2008).…”

Section: Introductionmentioning

confidence: 99%

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Cerato-platanin shows expansin-like activity on cellulosic materials

Baccelli

Luti

Bernardi

et al. 2013

Appl Microbiol Biotechnol

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Cerato-platanin (CP) is a non-catalytic protein with a double =β-barrel fold located in the cell wall of the phytopathogenic fungus Ceratocystis platani. CP is released during growth and induces defence-related responses in plants. CP is also the first member of the "cerato-platanin family" (CPF) (Pfam PF07249). In the CPF, the molecular mechanism of action on plants and above all the biological role in fungal life are little-known aspects. However, an expansin-like function has recently been suggested concerning CP. Expansin-like proteins have the ability to act non-hydrolytically on cellulose. In the present work, the expansin-like activity of CP and Pop1, a CP family member, was investigated. Like expansins, CP and Pop1 were able to weaken filter paper in a concentration-dependent manner and without the production of reducing sugars. A metal-dependent polysaccharide monooxygenase-like activity was excluded. The optimum of activity was pH5.0, 38°C. CP was also able to cause fragmentation of the crystalline cellulose Avicel and the breakage and defibration of cotton fibres. However, the interaction did not involve a stable bond with the substrates and CP did not significantly enhance the hydrolytic activity of cellulase. On the other hand, CP and Pop1 bound quickly to chitin. We consider CP as a novel one-domain expansin-like protein. We propose a structural role for CP in the fungal cell wall due to the ability to bind chitin, and hypothesize a functional role in the interaction of the fungus with the plant for the weakening activity shown on cellulose.

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Section: Discussionmentioning

confidence: 99%

Section: Binding To Polysaccharidesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Cerato-platanin shows expansin-like activity on cellulosic materials

Baccelli

Luti

Bernardi

et al. 2013

Appl Microbiol Biotechnol

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“…1.21) which hydrolyze soluble cellodextrins to glucose, mitigating CBH product inhibition arising from cellobiose (4,10,37,38,40). Hemicellulases, ligninases, and other secreted accessory proteins, such as swollenin, increase the accessibility of cellulose to these hydrolytic cellulase activities (10,2,15,19,27,29,39).…”

mentioning

confidence: 99%

Oxidoreductive Cellulose Depolymerization by the Enzymes Cellobiose Dehydrogenase and Glycoside Hydrolase 61

Langston

Shaghasi

Abbate

et al. 2011

Appl Environ Microbiol

377

344

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Several members of the glycoside hydrolase 61 (GH61) family of proteins have recently been shown to dramatically increase the breakdown of lignocellulosic biomass by microbial hydrolytic cellulases. However, purified GH61 proteins have neither demonstrable direct hydrolase activity on various polysaccharide or lignacious components of biomass nor an apparent hydrolase active site. Cellobiose dehydrogenase (CDH) is a secreted flavocytochrome produced by many cellulose-degrading fungi with no well-understood biological function. Here we demonstrate that the binary combination of Thermoascus aurantiacus GH61A (TaGH61A) and Humicola insolens CDH (HiCDH) cleaves cellulose into soluble, oxidized oligosaccharides. TaGH61A-HiCDH activity on cellulose is shown to be nonredundant with the activities of canonical endocellulase and exocellulase enzymes in microcrystalline cellulose cleavage, and while the combination of TaGH61A and HiCDH cleaves highly crystalline bacterial cellulose, it does not cleave soluble cellodextrins. GH61 and CDH proteins are coexpressed and secreted by the thermophilic ascomycete Thielavia terrestris in response to environmental cellulose, and the combined activities of T. terrestris GH61 and T. terrestris CDH are shown to synergize with T. terrestris cellulose hydrolases in the breakdown of cellulose. The action of GH61 and CDH on cellulose may constitute an important, but overlooked, biological oxidoreductive system that functions in microbial lignocellulose degradation and has applications in industrial biomass utilization.

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“…Despite the apparent lack of direct lytic activity on cellulose, the addition of T. reesei swollenin significantly increases the breakdown of filter paper by cellulases [99,100]. Swollenin from Aspergillus fumigatus is reported to have weak lytic activity on CMC but no apparent hydrolytic activity on microcrystalline cellulose, though treatment of microcrystalline cellulose with A. fumigatus swollenin reduced apparent microcrystalline cellulose particle size and potentiated breakdown of the cellulose by hydrolytic cellulases [101].…”

Section: Expansin Swollenin and Loosininmentioning

confidence: 99%

Biomass Converting Enzymes as Industrial Biocatalysts for Fuels and Chemicals: Recent Developments

2012

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Abstract:The economic utilization of abundant lignocellulosic biomass as a feedstock for the production of fuel and chemicals would represent a profound shift in industrial carbon utilization, allowing sustainable resources to substitute for, and compete with, petroleum based products. In order to exploit biomass as a source material for production of renewable compounds, it must first be broken down into constituent compounds, such as sugars, that can be more easily converted in chemical and biological processes. Lignocellulose is, unfortunately, a heterogeneous and recalcitrant material which is highly resistant to depolymerization. Many microorganisms have evolved repertoires of enzyme activities which act in tandem to decompose the various components of lignocellulosic biomass. In this review, we discuss recent advances in the understanding of these enzymes, with particular regard to those activities deemed likely to be applicable in commercialized biomass utilization processes.

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High-Level Expression and Efficient Purification of Bioactive Swollenin in Aspergillus oryzae

Cited by 23 publications

References 20 publications

Cerato-platanin shows expansin-like activity on cellulosic materials

Cerato-platanin shows expansin-like activity on cellulosic materials

Oxidoreductive Cellulose Depolymerization by the Enzymes Cellobiose Dehydrogenase and Glycoside Hydrolase 61

Biomass Converting Enzymes as Industrial Biocatalysts for Fuels and Chemicals: Recent Developments

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