Fungal Enzymes for Bio-Products from Sustainable and Waste Biomass

Gupta, Vijai Kumar; Kubicek, Christian P.; Berrin, Jean‐Guy; Wilson, David W.; Couturier, Marie; Berlin, Alex; Filho, Edivaldo Ximenes Ferreira; Ezeji, Thaddeus Chukwuemeka

doi:10.1016/j.tibs.2016.04.006

Cited by 246 publications

(137 citation statements)

References 87 publications

Supporting

Mentioning

128

Contrasting

Unclassified

Order By: Relevance

“…4a. Longer chain oligomers—cellononaose and celloheptaose were more energetically favored than dimer—cellobiose; this is characteristic of GH7 cellobiohydrolases [2, 3, 6–8, 11, 12, 17, 40, 41]. Of the two proteins under consideration, TrCBH1 seemed to be more energetically favored both on cellononaose as well as cellobiose, while no significant difference was observed on celloheptaose.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Comparative insights into the saccharification potentials of a relatively unexplored but robust Penicillium funiculosum glycoside hydrolase 7 cellobiohydrolase

Ogunmolu

Jagadeesha

Kumar

et al. 2017

Biotechnol Biofuels

View full text Add to dashboard Cite

BackgroundGH7 cellobiohydrolases (CBH1) are vital for the breakdown of cellulose. We had previously observed the enzyme as the most dominant protein in the active cellulose-hydrolyzing secretome of the hypercellulolytic ascomycete—Penicillium funiculosum (NCIM1228). To understand its contributions to cellulosic biomass saccharification in comparison with GH7 cellobiohydrolase from the industrial workhorse—Trichoderma reesei, we natively purified and functionally characterized the only GH7 cellobiohydrolase identified and present in the genome of the fungus.ResultsThere were marginal differences observed in the stability of both enzymes, with P. funiculosum (PfCBH1) showing an optimal thermal midpoint (T m) of 68 °C at pH 4.4 as against an optimal T m of 65 °C at pH 4.7 for T. reesei (TrCBH1). Nevertheless, PfCBH1 had an approximate threefold lower binding affinity (K m), an 18-fold higher turnover rate (k cat), a sixfold higher catalytic efficiency as well as a 26-fold higher enzyme-inhibitor complex equilibrium dissociation constant (K i) than TrCBH1 on p-nitrophenyl-β-d-lactopyranoside (pNPL). Although both enzymes hydrolyzed cellooligomers (G2–G6) and microcrystalline cellulose, releasing cellobiose and glucose as the major products, the propensity was more with PfCBH1. We equally observed this trend during the hydrolysis of pretreated wheat straws in tandem with other core cellulases under the same conditions. Molecular dynamic simulations conducted on a homology model built using the TrCBH1 structure (PDB ID: 8CEL) as a template enabled us to directly examine the effects of substrate and products on the protein dynamics. While the catalytic triads—EXDXXE motifs—were conserved between the two enzymes, subtle variations in regions enclosing the catalytic path were observed, and relations to functionality highlighted.ConclusionTo the best of our knowledge, this is the first report about a comprehensive and comparative description of CBH1 from hypercellulolytic ascomycete—P. funiculosum NCIM1228, against the backdrop of the same enzyme from the industrial workhorse—T. reesei. Our study reveals PfCBH1 as a viable alternative for CBH1 from T. reesei in industrial cellulase cocktails.Electronic supplementary materialThe online version of this article (doi:10.1186/s13068-017-0752-x) contains supplementary material, which is available to authorized users.

show abstract

Section: Resultsmentioning

confidence: 99%

“…The tunnel-bearing structures allow the enzyme to slide along the cellulose chain to the next cleavage site as the product is released [2]. GH7 CBHs catalytic domain shares a common β-jelly roll fold with two largely antiparallel β-sheets packing face to face to form a curved β-sandwich.…”

Section: Introductionmentioning

confidence: 99%

Comparative insights into the saccharification potentials of a relatively unexplored but robust Penicillium funiculosum glycoside hydrolase 7 cellobiohydrolase

Ogunmolu

Jagadeesha

Kumar

et al. 2017

Biotechnol Biofuels

View full text Add to dashboard Cite

show abstract

“…Figure 3 shows in vitro growth of lignin degrading fungi [46]. Soft rot fungi are no doubt the most efficient fungi to degrade lignin in mixed microbial populations [25,47].…”

Section: Soft-rot Fungimentioning

confidence: 99%

Lignin Degradation by Fungal Pretreatment: A Review

Madadi¹,

Abbas²

2017

J Plant Pathol Microbiol

View full text Add to dashboard Cite

Lignin is regarded as the most plentiful aromatic polymer contains both non-phenolic and phenolic structures. It makes the integral part of secondary wall and plays a significant role in water conduction in vascular plants. Many fungi, bacteria and insects have ability to decrease this lignin by producing enzymes. Among these fungi are the major player in degradation of lignin. These fungi produce enzymes such as lignin peroxidases and laccases. The well-known fungi which degrades lignin are white, brown, soft-rot fungi, and deuteromycetes. Currently these fungi are utilized to reduce lignin to produce ecofriendly bioenergy. The primary aim of this paper is to describe the lignin degradation by biological pre-treatment using fungi (white-, brown-soft-rot fungi and molds), as well as biochemical application. Besides, Molecular methods and enzymes regulation engaged in fungal pre-treatment and some of the factors affecting pretreatment will also be briefly discussed.

show abstract

“…The breakdown of lignocellulose in the plant cell wall requires the recruitment of glycoside hydrolases with different mechanisms of action in a concerted action with ligninases (Gupta et al 2016). Moreover, pre-treatment using microbial enzymes for ethanol production is a promising technology due to its several advantages, like being an eco-friendly and economically viable strategy for enhancing enzymatic saccharification rates (Sindhu et al 2015).…”

Section: Introductionmentioning

confidence: 99%

Sugarcane bagasse as a source of carbon for enzyme production by filamentous fungi1

Ferreira

Dall'Antonia

Shiga

et al. 2018

Hoehnea

View full text Add to dashboard Cite

-(Sugarcane bagasse as a source of carbon for enzyme production by fi lamentous fungi). The aim of the present work was to assess the enzymatic activity of six strains of fi lamentous fungi grown in liquid media containing 1% sugarcane bagasse as the sole carbon source. All fungal strains were able to use this agro-industrial residue, producing various types of enzymes, such as cellulases, xylanases, amylases, pectinases, and laccases. However, Aspergillus japonicus Saito was the most effi cient producer, showing the highest enzymatic activity for laccase (395.73 U L -1 ), endo-β-1,4-xylanase (3.55 U mL -1 ) and β-xylosidase (9.74 U mL -1 ) at seven, fourteen and twenty-one days in culture, respectively. Furthermore, the endo-β-1,4-xylanases and β-xylosidases of A. japonicus showed maximum activity at 50°C, and pH 5.5 and pH 3.5-4.5, respectively. Thus, these results indicate that A. japonicus has a great biotechnological potential for the production of these enzymes using sugarcane bagasse as the sole source of carbon.

show abstract

Fungal Enzymes for Bio-Products from Sustainable and Waste Biomass

Cited by 246 publications

References 87 publications

Comparative insights into the saccharification potentials of a relatively unexplored but robust Penicillium funiculosum glycoside hydrolase 7 cellobiohydrolase

Comparative insights into the saccharification potentials of a relatively unexplored but robust Penicillium funiculosum glycoside hydrolase 7 cellobiohydrolase

Lignin Degradation by Fungal Pretreatment: A Review

Sugarcane bagasse as a source of carbon for enzyme production by filamentous fungi1

Contact Info

Product

Resources

About