Activated alginate-montmorillonite beads as an efficient carrier for pectinase immobilization

Mohammadi, Maryam; Heshmati, Maryam Khakbaz; Sarabandi, Khashayar; Fathi, Maryam; Lim, Loong‐Tak; Hamishehkar, Hamed

doi:10.1016/j.ijbiomac.2019.06.236

Cited by 41 publications

(18 citation statements)

References 49 publications

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“…The catalytic activity of an enzyme is influenced by pH because the enzyme-substrate interaction can be altered [54]. The effect of pH on immobilized enzymes must be evaluated considering the possibility of applying them on an industrial scale.…”

Section: Effect Of Phmentioning

confidence: 99%

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

et al. 2020

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In the present work the radish (Raphanus sativus L.) was used as the low-cost alternative source of peroxidase. The enzyme was immobilized in different supports: coconut fiber (CF), calcium alginate microspheres (CAMs) and silica SBA-15/albumin hybrid (HB). Physical adsorption (PA) and covalent binding (CB) as immobilization techniques were evaluated. Immobilized biocatalysts (IBs) obtained were physicochemical and morphologically characterized by SEM, FTIR and TGA. Also, optimum pH/temperature and operational stability were determined. For all supports, the immobilization by covalent binding provided the higher immobilization efficiencies—immobilization yield (IY%) of 89.99 ± 0.38% and 77.74 ± 0.42% for HB and CF, respectively. For CAMs the activity recovery (AR) was of 11.83 ± 0.68%. All IBs showed optimum pH at 6.0. Regarding optimum temperature of the biocatalysts, HB-CB and CAM-CB maintained the original optimum temperature of the free enzyme (40 °C). HB-CB showed higher operational stability, maintaining around 65% of the initial activity after four consecutive cycles. SEM, FTIR and TGA results suggest the enzyme presence on the IBs. Radish peroxidase immobilized on HB support by covalent binding is promising in future biotechnological applications.

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Section: Effect Of Phmentioning

confidence: 99%

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

et al. 2020

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“…Thus, the ions can be firmly connected and can form a mechanically stable nanocomposite. Some researchers have reported the immobilization of horseradish peroxidase, pectinase, and Candida rugosa lipase on Alg-/clay-based hydrogels for biotechnological applications [ 18 , 19 , 20 ]. Lysozyme is one of the most abundant antimicrobial proteins.…”

Section: Introductionmentioning

confidence: 99%

Composite Aerogel Comprised of Sodium Alginate and Bentonite via Supercritical CO2 Drying: An Efficient Adsorbent for Lysozyme

Zhao

Cao

Yang

2022

Gels

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To meet the demand for the separation of specific substances, the construction of porous composite aerogels with a high specific surface area and a strong adsorption capacity is still a challenge. Herein, a sodium alginate/bentonite composite aerogel was efficiently prepared through supercritical fluid drying. The aerogel’s volume shrank less during supercritical drying, maintaining its original three-dimensional mesh structure. The resulting aerogel had a large specific surface area (445 m2/g), a low density (0.059 g/cm3), and a large pore volume (3.617 cm3/g). Due to the fixation and intercalation effects, bentonite was uniformly dispersed in the sodium alginate matrixes. The adsorption of lysozyme by the composite aerogel was evaluated, and the results showed that the optimal adsorption pH was 8 when the pH of the phosphoric acid buffer solution was between pH = 5 and 8.5. The time for adsorption to reach equilibrium was 8 h. The adsorption capacity increased with the increase in bentonite content, and when the initial concentration of lysozyme was from 0.2 to 1.2 g/L, the adsorption capacity first increased and then stabilized, and the maximum adsorption amount was 697 mg/g. The adsorption behavior was simulated in the isothermal region, and the linear correlation coefficient of Langmuir isothermal adsorption fitting was found to be 0.997. Thus, this composite aerogel with strong adsorption capacity can be used as a good alternative to enzymatic adsorbents or immobilized materials.

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“…In the encapsulation process, alginate is the preferred material because of its unique properties like mild gelation conditions, low cost, non-toxic, easy formulation, biocompatibility, and it also prevents microbial attack. Here we mixed alginate with clay to overcome disadvantages like excessive diffusion of enzyme from calcium alginate gel due to large pore size and weak mechanical strength (6) .…”

Section: Introductionmentioning

confidence: 99%

Kurthia gibsonii Mb126 immobilised chitinase against Aspergillus flavus, a fungal pathogen linked to lemon postharvest deterioration

Paul¹,

Mini²,

Benn³

et al. 2022

IJST

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Background of the study: As fungi become resistant to commonly used pesticides, fungicides are becoming not only more expensive, but also less effective in controlling postharvest infections. New chitinase immobilisation techniques are urgently needed to minimize enzyme costs while enhancing bio catalytic performance, antifungal activity, enzyme stability, and reusability. Objectives: The objective of this study was to immobilise chitinase of Kurthia gibsonii Mb126 by entrapping it in calcium alginate beads and to analyse its antifungal activities against Aspergillus flavus. Methods: The optimal parameters influencing the immobilization process and the characteristics of soluble and immobilised chitinase of K. gibsonii Mb126 were analysed. The antifungal activities of immobilised and free chitinase of K. gibsonii Mb126 against A. flavus, which was isolated from decayed lemon fruit, were performed using the agar-disk diffusion method. Free chitinase 25.0 mL (0.8 U/mL) and immobilised chitinase 0.06 g (specific activity 124-192 U/mg) were treated on separate lemon fruits for testing antifungal activity against A. flavus. Findings: K. gibsonii Mb126 chitinase was immobilised perfectly in calcium alginate beads. After optimising process parameters of immobilisation (sodium alginate concentration 3%, calcium chloride 0.2 M, 120 min. curing time), the specific activity of K. gibsonii Mb126 immobilised chitinase improved to 11.9-fold greater than the free form of chitinase and the immobilisation yield increased to 84%. It was observed that the thermal stability and storage stability of immobilised chitinase were better than those of free enzymes. The immobilised chitinase could be reused, and it retained 78% activity even after 16 cycles. The surface morphology of immobilised chitinase was observed in a scanning electron microscope at different magnification powers. Enzyme kinetics was studied and compared with that of its chitinase soluble counterpart. An in vitro study demonstrated that immobilised chitinase of K. gibsonii Mb126 has higher antifungal activity against A. flavus. In vivo experimental study of the https://www.indjst.org/ 136

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Activated alginate-montmorillonite beads as an efficient carrier for pectinase immobilization

Cited by 41 publications

References 49 publications

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

Immobilization of Low-Cost Alternative Vegetable Peroxidase (Raphanus sativus L. peroxidase): Choice of Support/Technique and Characterization

Composite Aerogel Comprised of Sodium Alginate and Bentonite via Supercritical CO2 Drying: An Efficient Adsorbent for Lysozyme

Kurthia gibsonii Mb126 immobilised chitinase against Aspergillus flavus, a fungal pathogen linked to lemon postharvest deterioration

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