Characterization of β-mannanase extracted from a novel <i>Streptomyces</i> species Alg-S25 immobilized on chitosan nanoparticles

Mohapatra, Bidyut R.

doi:10.1080/13102818.2020.1858158

Cited by 27 publications

(20 citation statements)

References 65 publications

(92 reference statements)

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“…The immobilized enzyme depicted enhanced activity in the pH range of 5.5–7. This enhanced activity of immobilized enzyme toward neutral pH may be as a result of the covalent binding of the enzyme with chitosan and change in the immediate microenvironment of the enzyme [ 8 ]. Our observations were in congruence with the findings of Mohapatra et al, who demonstrated no change in the optimum pH of β-mannanase from Streptomyces spp.…”

Section: Resultsmentioning

confidence: 99%

“…Alg-S25 after immobilization on chitosan nanoparticles [ 53 ]. Similarly, the optimum pH of bovine liver catalase upon immobilization on chitosan beads was found be to be same as its native form [ 8 ]. However, there are many reports where the optimum pH of the enzyme shifted after immobilization on the chitosan beads.…”

Section: Resultsmentioning

confidence: 99%

“…Despite the versatility of β-mannanase, the use of these enzymes in soluble form at the industrial scale has some limitations including low stability, unmanageable recovery and reuse, short shelf life, difficulty in handling, and loss of activity at prolonged operational conditions [ 8 ]. However, immobilization of enzymes on or into solid matrixes can address these issues.…”

Section: Introductionmentioning

confidence: 99%

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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: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

et al. 2022

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“…To provide Ge@MIL with stable and high enzyme activity, we used lignin in biomass as a substrate for β-mannanase immobilization. 11 The synthesis method was based on batch processing techniques; therefore, it can be produced on a large scale. In addition, we explored an efficient and convenient method that led to tight tuning over the surface coating of Ge@MIL by water-in-oil (w/o) emulsion.…”

Section: Introductionmentioning

confidence: 99%

“…Ge@MIL synthesized in our study is distinguished by its temperature sensitivity, enzyme immobilization, and complete biodegradability. To provide Ge@MIL with stable and high enzyme activity, we used lignin in biomass as a substrate for β-mannanase immobilization . The synthesis method was based on batch processing techniques; therefore, it can be produced on a large scale.…”

Section: Introductionmentioning

confidence: 99%

Surface Gelatin-Coated β-Mannanase-Immobilized Lignin for Delayed Release of β-Mannanase to Remediate Guar-Based Fracturing Fluid Damage

Cong

et al. 2022

ACS Omega

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Herein, we developed an efficient and convenient method to address the problem of thickener decomposition in the low- permeability oilfield production process. It is crucial to design breakers that reduce viscosity by delaying thickener decomposition in appropriate environments. By using lignin in biomass as a substrate for β-mannanase immobilization (MIL), we fabricated a gel breaker, surface gelatin-coated β-mannanase-immobilized lignin (Ge@MIL). Through experiments and performance tests, we confirmed that the prepared Ge@MIL can release enzymes at a specific temperature, meanwhile having temperature-sensitive phase change properties and biodegradability. The results also show the tight tuning over the surface coating of Ge@MIL by a water-in-oil emulsion. Therefore, the prepared Ge@MIL has a promising application in the field of oil extraction as a green and efficient temperature-sensitive sustained-release capsule.

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Marine Polysaccharides: Occurrence, Enzymatic Degradation and Utilization

2021

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Macroalgae species are fast growing and their polysaccharides are already used as food ingredient due to their properties as hydrocolloids or they have potential high value bioactivity. The degradation of these valuable polysaccharides to access the sugar components has remained mostly unexplored so far. One reason is the high structural complexity of algal polysaccharides, but also the need for suitable enzyme cocktails to obtain oligo‐ and monosaccharides. Among them, there are several rare sugars with high value. Recently, considerable progress was made in the discovery of highly specific carbohydrate‐active enzymes able to decompose complex marine carbohydrates such as carrageenan, laminarin, agar, porphyran and ulvan. This minireview summarizes these achievements and highlights potential applications of the now accessible abundant renewable resource of marine polysaccharides.

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Characterization of β-mannanase extracted from a novel Streptomyces species Alg-S25 immobilized on chitosan nanoparticles

Cited by 27 publications

References 65 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

Surface Gelatin-Coated β-Mannanase-Immobilized Lignin for Delayed Release of β-Mannanase to Remediate Guar-Based Fracturing Fluid Damage

Marine Polysaccharides: Occurrence, Enzymatic Degradation and Utilization

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