Purification, characterization and thermodynamic analysis of cellulases produced from Thermomyces dupontii and its industrial applications

Nisar, Kinza; Abdullah, Rasedee; Kaleem, Afshan; Iqtedar, Mehwish; Aftab, Mahwish; Saleem, Faiza

doi:10.1016/j.sjbs.2022.103483

Cited by 18 publications

(7 citation statements)

References 27 publications

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“…As shown in Table 3 , the apparent K m values of the recombinant xanthanases fused with CBMs here were significantly lower than that of Mi Xen-CD, suggesting high affinities of both Psp CBM84 and Mi CBMx toward xanthan. In addition, due to the similarity of the main chain structure of xanthan and cellulose, the K m value of some endocellulase can be used to evaluate the endotype xanthanases, such as the cellulases from Aspergillus niger [ 36 ], Thermomyces duponti [ 37 ] and Bacillus sp., respectively [ 38 ], the K m of which are about 0.23 g/L–0.8 g/L, which further proves the feasibility of our kinetic model. The results were also in consistent with surface plasmon resonance (SPR) analysis ( Figure 5 ).…”

Section: Resultsmentioning

confidence: 99%

An Insight into the Essential Role of Carbohydrate-Binding Modules in Enzymolysis of Xanthan

Wang

et al. 2023

IJMS

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To date, due to the low accessibility of enzymes to xanthan substrates, the enzymolysis of xanthan remains deficient, which hinders the industrial production of functional oligoxanthan. To enhance the enzymatic affinity against xanthan, the essential role of two carbohydrate binding modules—MiCBMx and PspCBM84, respectively, derived from Microbacterium sp. XT11 and Paenibacillus sp. 62047—in catalytic properties of endotype xanthanase MiXen were investigated for the first time. Basic characterizations and kinetic parameters of different recombinants revealed that, compared with MiCBMx, PspCBM84 dramatically increased the thermostability of endotype xanthanase, and endowed the enzyme with higher substrate affinity and catalytic efficiency. Notably, the activity of endotype xanthanase was increased by 16 times after being fused with PspCBM84. In addition, the presence of both CBMs obviously enabled endotype xanthanase to produce more oligoxanthan, and xanthan digests prepared by MiXen-CBM84 showed better antioxidant activity due to the higher content of active oligosaccharides. The results of this work lay a foundation for the rational design of endotype xanthanase and the industrial production of oligoxanthan in the future.

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Section: Resultsmentioning

confidence: 99%

An Insight into the Essential Role of Carbohydrate-Binding Modules in Enzymolysis of Xanthan

Wang

et al. 2023

IJMS

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“…7%, respectively, was achieved(Nisar et al 2022). Further the molecular weight of endoglucanase (37 kDa) and betaglucosidase (66 kDa) was determined by SDS-PAGE.…”

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confidence: 94%

“…A cellulase from A. aculeatus PN14 was puri ed using ammonium sulphate precipitation, diethyl-aminoethyl-sephadex chromatography and dialysis (Nargotra et al 2022a). Similarly, Nisar et al (2022) puri ed endoglucanases and betaglucosidases from Thermomyces dupontii by ammonium sulfate precipitation followed by anion exchange and gel ltration chromatography. Cellulase and pectinase from Mucor circinelloides and Mucor hiemalis were partially puri ed using acetone concentration method (Al Mousa et al 2022).…”

Section: Introductionmentioning

confidence: 99%

“…Cellulases have got vast application potential for a wide range of industries viz. food/feed, brewery, winery, pulp and paper, textile, detergent, biofuel, agriculture, and others (Haldar et al 2022; Nisar et al 2022). Three different type of cellulases i.e.…”

Section: Introductionmentioning

confidence: 99%

“…2018).A cellulase, puri ed from a fungus Trichoderma longibrachiatum exhibited optimum pH of 4.8 with substantial stability at pH 3-6(Pachauri et al 2020). Puri ed endoglucanases and betaglucosidases from Thermomyces dupontii showed highest catalytic activity at pH 5.5 and remarkable stability over pH 4-6(Nisar et al 2022). A puri ed endoglucanase from Aspergillus niger had pH optima of 4.0, and the activity declined drastically on either side of this pH(Sulyman et al 2020).…”

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confidence: 99%

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Purification of ionic liquid stable Aspergillus assiutensis VS34 cellulase, and generation of nanobiocatalysts for potential biomass conversion to biofuel

Sharma,

Nargotra,

Sharma

et al. 2023

Preprint

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Ionic liquids (ILs) have gained immense attention as eco-friendly solvents for pretreatment of lignocellulosics for their potential bioconversion to biofuels, bio-chemicals, and other products. However, for saccharification of IL-pretreated biomass IL-stable cellulases are desired. IL-stable cellulase and xylanase enzyme preparation developed from a previously isolated Aspergillus assiutensis VS34 was used for saccharification of IL-pretreated biomass. Current study reports the purification of IL-stable cellulase (CMCase) from A. assiutensis VS34 based on salt precipitation and ion exchange chromatography. Functionality of the purified cellulase (2.10-fold) was observed by native-PAGE and zymography, and the molecular weight (27 kDa) was assayed by SDS-PAGE. Though optimum temperature and pH of CMCase was 50℃ and 6.0, respectively, but the enzyme showed considerable activity and stability over a wide range of temperature (40–80℃, 72–99%) and pH (3–11, 60–95%). The activity of enzymes was enhanced by certain metal ions (Ca2+, Cu2+, Mn2+, Mg2+, and Co2+), but decreased considerably with Hg2+. Km and Vmax of CMCase were 6.996 mg/ml and 16.103 µmol/min/mg, respectively. Process-apt properties of A. assiutensis VS34 CMCase reflect its application potential for a variety of processes including biomass conversion. Submerged fermentation was executed using A. assiutensis VS34 in wheat bran medium and a combined cellulase and xylanase preparation developed was acetone-concentrated. The nanobiocatalysts were prepared by immobilization of concentrated cellulase/xylanase enzyme preparation on magnetic nanoparticles (efficiency 78.04% and 58.44%, respectively), and were examined for their saccharification potential for IL-pretreated sugarcane bagasse for repeated cycles.

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Microbial Cellulases and Their Characterization for Industrial Applications

Basak,

Ghosh

2024

Environmental Science and Engineering

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Purification, characterization and thermodynamic analysis of cellulases produced from Thermomyces dupontii and its industrial applications

Cited by 18 publications

References 27 publications

An Insight into the Essential Role of Carbohydrate-Binding Modules in Enzymolysis of Xanthan

An Insight into the Essential Role of Carbohydrate-Binding Modules in Enzymolysis of Xanthan

Purification of ionic liquid stable Aspergillus assiutensis VS34 cellulase, and generation of nanobiocatalysts for potential biomass conversion to biofuel

Microbial Cellulases and Their Characterization for Industrial Applications

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