Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin

Awad, Ghada E. A.; Aty, Abeer A. Abd El; Shehata, Abeer N.; Hassan, E. A.; Elnashar, Magdy M. M.

doi:10.1007/s13205-015-0338-x

Cited by 42 publications

(25 citation statements)

References 30 publications

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“…However, a reduction of the optimal pH value by immobilization of the enzyme was recorded for the naringinase from Penicillium decumbens immobilized on celite—from pH 4.0 to 3.5 [28]. The lowering of optimum pH from 4.5 to 4.0 as a result of naringinase immobilization was also observed by Puri et al [29] and Awad et al [56]. In view of the fact that most fruit juices show acidic pH values, the low pH values are an important factor for the possible application of immobilized naringinase [56].…”

Section: Resultsmentioning

confidence: 73%

Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Bodakowska-Boczniewicz

Garncarek

2019

Molecules

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Naringinase is an enzyme complex which exhibits α-l-rhamnosidase and β-d-glucosidase activity. This enzymatic complex catalyzes the hydrolysis of naringin (4′,5,7-trihydroxy flavanone 7-rhamnoglucoside), the main bittering component in grapefruit. Reduction of the level of this substance during the processing of juice has been the focus of many studies. The aim of the study was the immobilization of naringinase on chitosan microspheres activated with glutaraldehyde and, finally, the use of such immobilized enzyme for debittering grapefruit juice. The effect of naringinase concentration and characterization of the immobilized enzyme compared to the soluble enzyme were investigated. The maximum activity was observed at optimum pH 4.0 for both free and immobilized naringinase. However, the optimum temperature was shifted from 70 to 40 °C upon immobilization. The KM value of the immobilized naringinase was higher than that of soluble naringinase. The immobilization did not change the thermal stability of the enzyme. The immobilized naringinase had good operational stability. This preparation retained 88.1 ± 2.8% of its initial activity after ten runs of naringin hydrolysis from fresh grapefruit juice. The results indicate that naringinase immobilized on chitosan has potential applicability for debittering and improving the sensory properties of grapefruit juices.

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Section: Resultsmentioning

confidence: 73%

Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Bodakowska-Boczniewicz

Garncarek

2019

Molecules

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“…In general, the size of the beads ranged from (2.0 ± 0.4) to (2.5 ± 0.2) mm for the hydrated and (1.1 ± 0.2) to (1.7 ± 0.2) mm for the dried beads. The size and shape of the beads should be influenced by internal and external factors including surface tension of alginate solution and gelation bath, collecting distance, CaCl 2 concentration, needle diameter, M/G ratio, distribution in alginate chains, and stirring rate of gelation bath [68,69]. When the solution droplet hits and enters in the gelling bath, there are competing forces between the viscous surface tension and impact-drag forces to maintain the droplet shape [65].…”

Section: Thermogravimetric Analysismentioning

confidence: 99%

Biodegradation of Crystalline Cellulose Nanofibers by Means of Enzyme Immobilized-Alginate Beads and Microparticles

et al. 2020

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Recent advances in nanocellulose technology have revealed the potential of crystalline cellulose nanofibers to reinforce materials which are useful for tissue engineering, among other functions. However, the low biodegradability of nanocellulose can possess some problems in biomedical applications. In this work, alginate particles with encapsulated enzyme cellulase extracted from Trichoderma reesei were prepared for the biodegradation of crystalline cellulose nanofibers, which carrier system could be incorporated in tissue engineering biomaterials to degrade the crystalline cellulose nanoreinforcement in situ and on-demand during tissue regeneration. Both alginate beads and microparticles were processed by extrusion-dropping and inkjet-based methods, respectively. Processing parameters like the alginate concentration, concentration of ionic crosslinker Ca2+, hardening time, and ionic strength of the medium were varied. The hydrolytic activity of the free and encapsulated enzyme was evaluated for unmodified (CNFs) and TEMPO-oxidized cellulose nanofibers (TOCNFs) in suspension (heterogeneous conditions); in comparison to solubilized cellulose derivatives (homogeneous conditions). The enzymatic activity was evaluated for temperatures between 25–75 °C, pH range from 3.5 to 8.0 and incubation times until 21 d. Encapsulated cellulase in general displayed higher activity compared to the free enzyme over wider temperature and pH ranges and for longer incubation times. A statistical design allowed optimizing the processing parameters for the preparation of enzyme-encapsulated alginate particles presenting the highest enzymatic activity and sphericity. The statistical analysis yielded the optimum particles characteristics and properties by using a formulation of 2% (w/v) alginate, a coagulation bath of 0.2 M CaCl2 and a hardening time of 1 h. In homogeneous conditions the highest catalytic activity was obtained at 55 °C and pH 4.8. These temperature and pH values were considered to study the biodegradation of the crystalline cellulose nanofibers in suspension. The encapsulated cellulase preserved its activity for several weeks over that of the free enzyme, which latter considerably decreased and practically showed deactivation after just 10 d. The alginate microparticles with their high surface area-to-volume ratio effectively allowed the controlled release of the encapsulated enzyme and thereby the sustained hydrolysis of the cellulose nanofibers. The relative activity of cellulase encapsulated in the microparticles leveled-off at around 60% after one day and practically remained at that value for three weeks.

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“…A similar strategy was applied in the case of crude naringinase from A. niger immobilized in PEI-activated alginate beads, but in this case, glutaraldehyde was used as a stabilizing agent [ 64 ]. Additionally, Ondul et al [ 65 ] immobilized lipase on cotton fabric fibers with adsorbed PEI, additionally stabilized with glutaraldehyde.…”

Section: Resultsmentioning

confidence: 99%

“…Awad et al [ 64 ] also noted a decrease in the optimal pH value of naringinase from A. niger after its covalent binding on the alginate carrier hardened with polyethyleneimine and glutaraldehyde.…”

Section: Resultsmentioning

confidence: 99%

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Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

Bodakowska-Boczniewicz

Garncarek

2020

Molecules

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Naringinase is an enzymatic complex used in the deglycosylation of compounds with a high application potential in the food and pharmaceutical industries. The aim of the study was to immobilize naringinase from Aspergillus niger KMS on a magnetic carrier obtained on the basis of carob gum activated by polyethyleneimine. Response surface methodology was used to optimize naringinase immobilization taking into account the following factors: pH, immobilization time, initial concentration of naringinase and immobilization temperature. The adsorption of the enzyme on a magnetic carrier was a reversible process. The binding force of naringinase was increased by crosslinking the enzyme with the carrier using dextran aldehyde. The crosslinked enzyme had better stability in an acidic environment and at a higher temperature compared to the free form. The immobilization and stabilization of naringinase by dextran aldehyde on the magnetic polysaccharide carrier lowered the activation energy, thus increasing the catalytic capacity of the investigated enzyme and increasing the activation energy of the thermal deactivation process, which confirms higher stability of the immobilized enzyme in comparison with free naringinase. The preparation of crosslinked naringinase retained over 80% of its initial activity after 10 runs of naringin hydrolysis from fresh and model grapefruit juice.

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Covalent immobilization of microbial naringinase using novel thermally stable biopolymer for hydrolysis of naringin

Cited by 42 publications

References 30 publications

Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Biodegradation of Crystalline Cellulose Nanofibers by Means of Enzyme Immobilized-Alginate Beads and Microparticles

Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

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