Recent progress in key lignocellulosic enzymes: Enzyme discovery, molecular modifications, production, and enzymatic biomass saccharification

Li, Yangyang; Song, Weiyan; Han, Xuyue; Wang, Yachan; Rao, Shengqi; Zhang, Quan; Zhou, Jingwen; Li, Jianghua; Liu, Song; Du, Guocheng

doi:10.1016/j.biortech.2022.127986

Cited by 31 publications

(6 citation statements)

References 146 publications

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“…Previously reported β-glucanases have diverse behaviors under the influence of metal ions and organic compounds. The activity of an exo-β-1,3-glucanase from the moose rumen microbiome [29] more than doubled in the presence of zinc ions, retaining normal activity in the presence of EDTA, propanol, and butanol. In contrast, the activity of IDSGLUC9-4 slightly decreased in the presence of 20 mM EDTA (p < 0.05) but lost >50% of its activity in the presence of DMSO and propanol.…”

Section: A C C E P T E Dmentioning

confidence: 99%

Expression and characterization of a novel microbial GH9 glucanase, IDSGLUC9-4, isolated from sheep rumen

Zhu,

Bai,

et al. 2024

Anim Biosci

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This study aimed to identify and characterize a novel endo-β-glucanase, IDSGLUC9-4, from the rumen metatranscriptome of Hu sheep. Methods:A novel endo-β-glucanase, IDSGLUC9-4, was heterologously expressed in Escherichia coli and biochemically characterized. The optimal temperature and pH of recombinant IDSGLUC9-4 were determined. Subsequently, substrate specificity of the enzyme was assessed using mixed-linked glucans including barley β-glucan and Icelandic moss lichenan. Thin-layer chromatography (TLC), high-performance liquid chromatography (HPLC), matrix assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF) analyses were conducted to determine the products released from polysaccharides and cello-oligosaccharides substrates. Results:The recombinant IDSGLUC9-4 exhibited temperature and pH optima of 40 °C and pH 6.0, respectively. It exclusively hydrolyzed mixed-linked glucans, with significant activity observed for barley β-glucan (109.59 ± 3.61 μmol•mg -1 •min -1 ) and Icelandic moss lichenan (35.35 ± 1.55 μmol•mg -1 •min -1 ). TLC and HPLC analyses revealed that IDSGLUC9-4 primarily released cellobiose, cellotriose, and cellotetraose from polysaccharide substrates. Furthermore, after 48 h of reaction, IDSGLUC9-4 removed most of the glucose, indicating transglycosylation activity alongside its endo-glucanase activity.

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Section: A C C E P T E Dmentioning

confidence: 99%

Expression and characterization of a novel microbial GH9 glucanase, IDSGLUC9-4, isolated from sheep rumen

Zhu,

Bai,

et al. 2024

Anim Biosci

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“…In recent years, researchers have used methods such as the optimization of reaction conditions, including the search for reaction mediators or inducers, the use of surfactants, the immobilization of enzymes on matrices with various properties, and modifications of catalytic activity and substrate specificity using molecular biology and engineering techniques to increase enzyme activity [315,316].…”

Section: Improvement Of Catalytic Activity Of Laccasesmentioning

confidence: 99%

“…The cheapest way to overproduce enzymes is to optimize the fermentation conditions, and a spectacular increase in the amount of enzyme produced by a given microorganism can be achieved by changing just a few parameters. A modern method more and more willingly used to optimize the composition of media is the methodology of the response surface (RSM) [316]. With good results, RSM was used to optimize the production of laccase by A. bisporus CU13 [331]; Pseudolagarobasidium acaciicola AGST3 [332]; and Penicillium chrysogenum [225].…”

Section: Improvement Of Laccase Productivitymentioning

confidence: 99%

Biochemical Characteristics of Laccases and their Practical Application in the Removal of Xenobiotics from Waters

Gałązka¹,

Jankiewicz²,

Szczepkowski³

2023

Preprint

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Industrialization, intensive farming, rapid population growth and urbanization are the source of a large number of pollutants entering the environment. The current concentration of xenobiotics released into the environment exceeds its natural ability to decompose them. Enzymatic degradation of pollutants seems to be an environmentally friendly process. Due to the wide spectrum of substrate specificity, from inorganic compounds to high molecular weight organic compounds such as PAH or dyes, as well as favorable biochemical properties, laccase has been used in the biological removal of xenobiotics from the environment. It is important to understand the degradation mechanisms of pollutants and to evaluate the final products in terms of their toxicity. The laccase oxidizes the substrates with the simultaneous reduction of molecular oxygen to water, which is the purest reaction co-substrate. That is why it is called a green biocatalyst. The trend is an increase in the production of enzymes related to the intensive development of industry, bioremediation or synthetic chemistry. This leads to the search for laccases with greater activity and stability under extreme conditions. The potential of laccases to degrade xenobiotics can be promoted by improving enzymatic catalytic characterization using protein engineering and other genetic engineering methods.

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“…Renewable fuels and biobased products are continuously gaining attention due to the eventual shortage of fossil fuels and nonrenewable resources. Lignocellulosic biomass (LCB) is the most abundant source of fermentable sugars, − which can be used to produce biofuels like bioethanol or any other product obtained via fermentation . Modern integrated biorefineries that concentrate the production of biobased products and energy from LCB are in fast development nowadays .…”

Section: Introductionmentioning

confidence: 99%

Cellulose Enzymatic Saccharification Intensified by Nonionic Surfactants

Balbi

Fleite

Kildegaard

et al. 2023

Ind. Eng. Chem. Res.

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Enzymatic saccharification of cellulose is one of the bottlenecks of second-generation bioethanol production and other bioprocesses aimed at the use of lignocellulosic residues. Hence, it is crucial to find conditions and additives that can improve this process. In this work, the use of different nonionic surfactants was studied. The results demonstrate that all tested additives increase the initial rate of filter paper saccharification, with PEG 600 more than doubling the initial rate for two cellulose enzymatic cocktails. The highest effects were found with surfactants of linear structure, which likely better separate the filter paper cellulose fibers, allowing enzyme access. The effect of surfactants was larger for experiments without agitation. However, orbital agitation improved both the initial rate and yields. The effect of the gas–liquid interfacial area was negligible. Despite the beneficial trends found for the filter paper, no significant improvements were evidenced while adding surfactants to the saccharification of acid-oxidative pretreated biomass. Similarly, carboxymethyl cellulose saccharification was only marginally enhanced. Hence, the substrate structure and delignification method have a strong effect on the influence of surfactant addition and should be considered for deciding the saccharification media formulation.

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Recent progress in key lignocellulosic enzymes: Enzyme discovery, molecular modifications, production, and enzymatic biomass saccharification

Cited by 31 publications

References 146 publications

Expression and characterization of a novel microbial GH9 glucanase, IDSGLUC9-4, isolated from sheep rumen

Expression and characterization of a novel microbial GH9 glucanase, IDSGLUC9-4, isolated from sheep rumen

Biochemical Characteristics of Laccases and their Practical Application in the Removal of Xenobiotics from Waters

Cellulose Enzymatic Saccharification Intensified by Nonionic Surfactants

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