Applications of Microbial β-Mannanases

Dawood, Aneesa; Ma, Kesen

doi:10.3389/fbioe.2020.598630

Cited by 68 publications

(37 citation statements)

References 113 publications

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“…β-1,4-mannanase (mannan mannohydrolase, EC 3.2.1.78) is an endo-acting hydrolase that randomly cleaves the β-1,4-mannosidic linkages in the main chain of mannans (linear mannan, galactomannan, glucomannan, and galactoglucomannan), therefore producing mannooligosaccharides (MOS) of various lengths [ 5 ]. β-mannanase has wide industrial applications as it is used for the production of partially hydrolyzed guar gum, MOS, fruit juice clarification, paper/pulp bio-bleaching, synthesis of detergents, amelioration of animal or poultry feed, and saccharification of biomass [ 6 , 7 ].…”

Section: Introductionmentioning

confidence: 99%

Modifying Thermostability and Reusability of Hyperthermophilic Mannanase by Immobilization on Glutaraldehyde Cross-Linked Chitosan Beads

et al. 2022

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In the current study, the purified β-mannanase (Man/Cel5B) from Thermotoga maritima was immobilized on glutaraldehyde cross-linked chitosan beads. The immobilization of Man/Cel5B on chitosan beads was confirmed by Fourier-transform infrared spectroscopy (FTIR) and X-ray diffraction (XRD) analysis. After immobilization, the protein loading efficiency and immobilization yield were found to be 73.3% and 71.8%, respectively. The optimum pH for both free and immobilized enzymes was found to be pH 5.5. However, the optimum temperature of immobilized Man/Cel5B increased by 10 °C, from 85 °C (free Man/Cel5B) to 95 °C (Immobilized). The half-life of free and immobilized enzymes was found to be 7 h and 9 h, respectively, at 85 °C owing to the higher thermostability of immobilized Man/Cel5B. The increase in thermostability was also demonstrated by an increase in the energy of deactivation (209 kJmol−1) for immobilized enzyme compared to its native form (92 kJmol−1), at 85 °C. Furthermore, the immobilized Man/Cel5B displayed good operational stability as it retained 54% of its original activity after 15 repeated catalytic reactions concerning its free form.

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Section: Introductionmentioning

confidence: 99%

Modifying Thermostability and Reusability of Hyperthermophilic Mannanase by Immobilization on Glutaraldehyde Cross-Linked Chitosan Beads

et al. 2022

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“…[162] Lipases Food industry [149,150] Aspergillus sp., Bacillus sp., Rhizopus sp., Trichosporon sp., Lactobacillus sp., Penicillium sp., Pseudomonas sp. [149] Mannanases Food, animal feed, and biorefinery industries [163] Bacillus sp., Trichoderma sp., Aspergillus sp., Thermomyces sp., Rhizopus sp. [149] Pectinases Food and animal feed industry [149,150] Aspergillus sp., Rhizopus sp., Penicillium sp.…”

Section: Oxidoreductasesmentioning

confidence: 99%

Value-Added Products from Ethanol Fermentation—A Review

et al. 2021

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Global demand for renewable and sustainable energy is increasing, and one of the most common biofuels is ethanol. Most ethanol is produced by Saccharomyces cerevisiae (yeast) fermentation of either crops rich in sucrose (e.g., sugar cane and sugar beet) or starch-rich crops (e.g., corn and starchy grains). Ethanol produced from these sources is termed a first-generation biofuel. Yeast fermentation can yield a range of additional valuable co-products that accumulate during primary fermentation (e.g., protein concentrates, water soluble metabolites, fusel alcohols, and industrial enzymes). Distillers’ solubles is a liquid co-product that can be used in animal feed or as a resource for recovery of valuable materials. In some processes it is preferred that this fraction is modified by a second fermentation with another fermentation organism (e.g., lactic acid bacteria). Such two stage fermentations can produce valuable compounds, such as 1,3-propanediol, organic acids, and bacteriocins. The use of lactic acid bacteria can also lead to the aggregation of stillage proteins and enable protein aggregation into concentrates. Once concentrated, the protein has utility as a high-protein feed ingredient. After separation of protein concentrates the remaining solution is a potential source of several known small molecules. The purpose of this review is to provide policy makers, bioethanol producers, and researchers insight into additional added-value products that can be recovered from ethanol beers. Novel products may be isolated during or after distillation. The ability to isolate and purify these compounds can provide substantial additional revenue for biofuel manufacturers through the development of marketable co-products.

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“…A number of endo-β-1,4-mannanases (E.C. 3.2.1.78) have been characterized due to their potential applications in different sectors of industry including detergent, textile, food, animal feed, and bioethanol [ 8 ]. They hydrolyze internal backbone β-1,4-linkages in mannans including in substituted mannans such as galactomannans from carob/locust bean (low and high viscosity; CGM-lv and CGM-hv) and guar bean (guar gum; GG), as well as in the linear konjac glucomannan (KGM) containing β-1,4-linked mannose and glucose units.…”

Section: Introductionmentioning

confidence: 99%

Impact of Modular Architecture on Activity of Glycoside Hydrolase Family 5 Subfamily 8 Mannanases

Møller

2022

Molecules

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Glycoside hydrolase family 5 subfamily 8 (GH5_8) mannanases belong to Firmicutes, Actinomycetia, and Proteobacteria. The presence or absence of carbohydrate-binding modules (CBMs) present a striking difference. While various GH5_8 mannanases need a CBM for binding galactomannans, removal of the CBM did not affect activity of some, whereas it in other cases reduced the catalytic efficiency due to increased KM. Here, monomodular GH5_8 mannanases from Eubacterium siraeum (EsGH5_8) and Xanthomonas citri pv. aurantifolii (XcGH5_8) were produced and characterized to clarify if GH5_8 mannanases from Firmicutes and Proteobacteria without CBM(s) possess distinct properties. EsGH5_8 showed a remarkably high temperature optimum of 55 °C, while XcGH5_8 had an optimum at 30 °C. Both enzymes were highly active on carob galactomannan and konjac glucomannan. Notably, EsGH5_8 was equally active on both substrates, whereas XcGH5_8 preferred galactomannan. The KM values were comparable with those of catalytic domains of truncated GH5_8s, while the turn-over numbers (kcat) were in the higher end. Notably, XcGH5_8 bound to but did not degrade insoluble ivory nut mannan. The findings support the hypothesis that GH5_8 mannanases with CBMs target insoluble mannans found in plant cell walls and seeds, while monomodular GH5_8 members have soluble mannans and mannooligosaccharides as primary substrates.

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Applications of Microbial β-Mannanases

Cited by 68 publications

References 113 publications

Modifying Thermostability and Reusability of Hyperthermophilic Mannanase by Immobilization on Glutaraldehyde Cross-Linked Chitosan Beads

Modifying Thermostability and Reusability of Hyperthermophilic Mannanase by Immobilization on Glutaraldehyde Cross-Linked Chitosan Beads

Value-Added Products from Ethanol Fermentation—A Review

Impact of Modular Architecture on Activity of Glycoside Hydrolase Family 5 Subfamily 8 Mannanases

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