Discovery of extremophilic cellobiohydrolases from marine Aspergillus niger with computational analysis

Cai, Li-Nian; Lu, Tao; Lin, Dong‐Qiang; Yao, Shan‐Jing

doi:10.1016/j.procbio.2022.02.016

Cited by 3 publications

(2 citation statements)

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“…Our results indicated that the optimum pH for most of the lignocellulolytic degradation activities of Rio Tinto fungi, which included some Trichoderma and Talaromyces especies, was below 5, a result that, in general, agrees with the final pH of the growth medium and with the pH from which the environment the fungal strains were isolated. Some acidophilous fungi, mainly belonging to the Aspergillus or Thielavia genus, have been identified as producers of acidophilus cellulolytic enzymes (Sohail et al 2009;Cai et al 2022;Grigorevski-Lima et al 2009); however, our results fully support that organisms that inhabit Rio Tinto, an unusually acid environment, are a broad source for acidophilus enzymes.…”

Section: Effect Of the Ph On The Hydrolytic Activities Of Rio Tinto F...supporting

confidence: 45%

Rio Tinto as a niche for acidophilus enzymes of industrial relevance

Daddaoua

Álvarez

Oggerin

et al. 2023

Microbial Biotechnology

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Lignocellulosic residues are amongst the most abundant waste products on Earth. Therefore, there is an increasing interest in the utilization of these residues for bioethanol production and for biorefineries to produce compounds of industrial interest. Enzymes that breakdown cellulose and hemicellulose into oligomers and monosaccharides are required in these processes and cellulolytic enzymes with optimum activity at a low pH area are desirable for industrial processes. Here, we explore the fungal biodiversity of Rıo Tinto, the largest acidic ecosystem on Earth, as far as the secretion of cellulolytic enzymes is concerned. Using colorimetric and industrial substrates, we show that a high proportion of the fungi present in this extremophilic environment secrete a wide range of enzymes that are able to hydrolyze cellulose and hemicellulose at acidic pH (4.5-5). Shotgun proteomic analysis of the secretomes of some of these fungi has identified different cellulases and hemicellulolytic enzymes as well as a number of auxiliary enzymes. Supplementation of preindustrial cocktails from Myceliophtora with Rio Tinto secretomes increased the amount of monosaccharides released from corn stover or sugar cane straw. We conclude that the Rio Tinto fungi display a good variety of hydrolytic enzymes with high industrial potential.

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Section: Effect Of the Ph On The Hydrolytic Activities Of Rio Tinto F...supporting

confidence: 45%

Rio Tinto as a niche for acidophilus enzymes of industrial relevance

Daddaoua

Álvarez

Oggerin

et al. 2023

Microbial Biotechnology

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“…For this reason, annotation reliability for halotolerant enzymes using archive databases is often inadequate due to low levels of representation particularly for high confidence annotations from characterisationlevel proteins. The GH6 family CBH in particular is poorly represented in terms of functionally characterised proteins [35][36][37] with even fewer reports of halotolerant variants 38,39 . A correlation between thermostability and halotolerance has long been known eluded to [40][41][42] and recent engineering approaches have yielded simultaneous improvements in CBH thermostability and tolerance to ionic liquids and seawater 42 .…”

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confidence: 99%

Functional characterisation of a new halotolerant seawater active glycoside hydrolase family 6 cellobiohydrolase from a salt marsh

Leadbeater,

Bruce

2024

Sci Rep

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Realising a fully circular bioeconomy requires the valorisation of lignocellulosic biomass. Cellulose is the most attractive component of lignocellulose but depolymerisation is inefficient, expensive and resource intensive requiring substantial volumes of potable water. Seawater is an attractive prospective replacement, however seawater tolerant enzymes are required for the development of seawater-based biorefineries. Here, we report a halophilic cellobiohydrolase SMECel6A, identified and isolated from a salt marsh meta-exo-proteome dataset with high sequence divergence to previously characterised cellobiohydrolases. SMECel6A contains a glycoside hydrolase family 6 (GH6) domain and a carbohydrate binding module family 2 (CBM2) domain. Characterisation of recombinant SMECel6A revealed SMECel6A to be active upon crystalline and amorphous cellulose. Mono- and oligosaccharide product profiles revealed cellobiose as the major hydrolysis product confirming SMECel6A as a cellobiohydrolase. We show SMECel6A to be halophilic with optimal activity achieved in 0.5X seawater displaying 80.6 ± 6.93% activity in 1 × seawater. Structural predictions revealed similarity to a characterised halophilic cellobiohydrolase despite sharing only 57% sequence identity. Sequential thermocycling revealed SMECel6A had the ability to partially reversibly denature exclusively in seawater retaining significant activity. Our study confirms that salt marsh ecosystems harbour enzymes with attractive traits with biotechnological potential for implementation in ionic solution based bioprocessing systems.

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