Highly efficient, processive and multifunctional recombinant endoglucanase RfGH5_4 from Ruminococcus flavefaciens FD-1 v3 for recycling lignocellulosic plant biomasses

Gavande, Parmeshwar Vitthal; Nath, Priyanka; Kumar, Krishan; Ahmed, Nizam; Fontes, C.M.G.A.; Goyal, Arun

doi:10.1016/j.ijbiomac.2022.04.059

Cited by 8 publications

(3 citation statements)

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“…Cellulases are the most common enzymes used in industry [ 153 ]. They are classified into five major groups based on the type of reaction catalyzed: Endocellulases, which break down the β-1,4-polysaccharide linkages in cellulose to release cellodextrins [ 154 ]: Exocellulases, which depolymerize amorphous regions of cellulose, resulting in the formation of various oligomers, such as cellobiose [ 155 ]; β-glycosidases, which hydrolyze β-glycosidic bonds in one of the intermediates formed by the action of exoglucanases and lead to the synthesis of D-glucose and D-glucose 6-phosphate [ 156 ]; Oxidative cellulases, which depolymerize cellulose; Cellulose phosphorylases, which depolymerize cellulose by using phosphates [ 157 ]. …”

Section: Lignocellulosic Biorefineries and The Roles Of Lignocellulol...mentioning

confidence: 99%

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Engineered yeasts and lignocellulosic biomaterials: shaping a new dimension for biorefinery and global bioeconomy

Asemoloye,

Bello,

Oladoye

et al. 2023

Bioengineered

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The next milestone of synthetic biology research relies on the development of customized microbes for specific industrial purposes. Metabolic pathways of an organism, for example, depict its chemical repertoire and its genetic makeup. If genes controlling such pathways can be identified, scientists can decide to enhance or rewrite them for different purposes depending on the organism and the desired metabolites. The lignocellulosic biorefinery has achieved good progress over the past few years with potential impact on global bioeconomy. This principle aims to produce different bio-based products like biochemical(s) or biofuel(s) from plant biomass under microbial actions. Meanwhile, yeasts have proven very useful for different biotechnological applications. Hence, their potentials in genetic/metabolic engineering can be fully explored for lignocellulosic biorefineries. For instance, the secretion of enzymes above the natural limit (aided by genetic engineering) would speed-up the down-line processes in lignocellulosic biorefineries and the cost. Thus, the next milestone would greatly require the development of synthetic yeasts with much more efficient metabolic capacities to achieve basic requirements for particular biorefinery. This review gave comprehensive overview of lignocellulosic biomaterials and their importance in bioeconomy. Many researchers have demonstrated the engineering of several ligninolytic enzymes in heterologous yeast hosts. However, there are still many factors needing to be well understood like the secretion time, titter value, thermal stability, pH tolerance, and reactivity of the recombinant enzymes. Here, we give a detailed account of the potentials of engineered yeasts being discussed, as well as the constraints associated with their development and applications.

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Section: Lignocellulosic Biorefineries and The Roles Of Lignocellulol...mentioning

confidence: 99%

“…Endocellulases, which break down the β-1,4-polysaccharide linkages in cellulose to release cellodextrins [ 154 ]:…”

Section: Lignocellulosic Biorefineries and The Roles Of Lignocellulol...mentioning

confidence: 99%

Engineered yeasts and lignocellulosic biomaterials: shaping a new dimension for biorefinery and global bioeconomy

Asemoloye,

Bello,

Oladoye

et al. 2023

Bioengineered

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“…The first report of PEGs from Thermomonospora fusca was reported in 1993 (Irwin et al, 1993), followed by several others. The majority of PEGs studied so far belong to Clostridium sp., while Paenibacillus, Bacillus, Cellulomonas, Ruminococcus, and Thermobifida are among the other genera (Reverbel-Leroy et al, 1997;Wilson, 2004;Mejia-Castillo et al, 2008;Chiriac et al, 2010;Wu and Wu, 2020; 1 https://www.polarismarketresearch.com/industry-analysis/ laundry-detergent-market Gavande et al, 2022). The bi-functional PEGs, combined with other cellulases, are more suitable for cellulose-based bioprocess development for bioethanol generation (Akram et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

A thermo-alkali stable and detergent compatible processive β-1,4-glucanase from Himalayan Bacillus sp. PCH94

Thakur

Singh

2022

Front. Microbiol.

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Present study reports a novel and robust GH9 processive endoglucanase β-1,4-glucanase from Bacillus sp. PCH94 (EGaseBL) with thermo-alkali stable properties. The EGaseBL gene was cloned in pET-28b(+) and expressed in Escherichia coli BL21(DE3) cells. The recombinant protein was purified 94-fold with a yield of 67.8%. The biochemical characterization revealed an active enzyme at a wide pH (4.0–10.0) and temperature (4–100°C). It showed a Km and Vmax of 1.10 mg/ml and 208.24 IU/mg, respectively, using β-glucan as a substrate. The EGaseBL showed dual activities for endoglucanase (134.17 IU/mg) and exoglucanase (28.76 IU/mg), assayed using substrates β-glucan and Avicel, respectively. The enzyme is highly stable in neutral and alkaline pH and showed a half-life of 11.29 h, and 8.31 h in pH 7.0 and 9.0, respectively. The enzyme is also compatible with commercial detergents (Tide, Surf, Ghadi, Raj, and Healing tree) of the Indian market and retained > 85% enzyme activity. Concisely, robustness, extreme functionality, and detergent compatibility endorse EGaseBL as a potential bioresource for the detergent industry, in addition to its implications for the bioethanol industry.Highlights– Cloning, expression, and purification of putative novel GH9 family β-1,4-glucanase.– Processive endoglucanase with CBM3 domain and bi-functional (endo/exo) activity.– Broad pH-temperature active and stable enzyme.– Compatible with commercial detergent powders.

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Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2021–2022

Harvey

2024

Mass Spectrometry Reviews

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The use of matrix‐assisted laser desorption/ionization (MALDI) mass spectrometry for the analysis of carbohydrates and glycoconjugates is a well‐established technique and this review is the 12th update of the original article published in 1999 and brings coverage of the literature to the end of 2022. As with previous review, this review also includes a few papers that describe methods appropriate to analysis by MALDI, such as sample preparation, even though the ionization method is not MALDI. The review follows the same format as previous reviews. It is divided into three sections: (1) general aspects such as theory of the MALDI process, matrices, derivatization, MALDI imaging, fragmentation, quantification and the use of computer software for structural identification. (2) Applications to various structural types such as oligo‐ and polysaccharides, glycoproteins, glycolipids, glycosides and biopharmaceuticals, and (3) other general areas such as medicine, industrial processes, natural products and glycan synthesis where MALDI is extensively used. Much of the material relating to applications is presented in tabular form. MALDI is still an ideal technique for carbohydrate analysis, particularly in its ability to produce single ions from each analyte and advancements in the technique and range of applications show little sign of diminishing.

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Highly efficient, processive and multifunctional recombinant endoglucanase RfGH5_4 from Ruminococcus flavefaciens FD-1 v3 for recycling lignocellulosic plant biomasses

Cited by 8 publications

References 54 publications

Engineered yeasts and lignocellulosic biomaterials: shaping a new dimension for biorefinery and global bioeconomy

Engineered yeasts and lignocellulosic biomaterials: shaping a new dimension for biorefinery and global bioeconomy

A thermo-alkali stable and detergent compatible processive β-1,4-glucanase from Himalayan Bacillus sp. PCH94

Analysis of carbohydrates and glycoconjugates by matrix‐assisted laser desorption/ionization mass spectrometry: An update for 2021–2022

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