Preparation and characterization of sugilite glass from basalt for α-amylase immobilization, statistical optimization of the immobilization process and description of free and immobilized enzyme

Abdel-Hameed, Salwa A.M.; Ahmed, Samia A.; Mostafa, Faten A.; Almasarawi, Ola N; Wahab, Walaa A. Abdel

doi:10.1016/j.heliyon.2022.e09960

Cited by 14 publications

(6 citation statements)

References 35 publications

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“…This implies the immobilized β-gal on Alg–TW/PEI/GA carrier had an excellent durability, recovery, and operational stability. Our finding is superior to that given by Ansari et al [ 25 ] who suggested that, the reusability of immobilized β-gal exhibited 89% residual activity after consecutive 5 cycles. On the other hand, the immobilized β-gal retained more than 90% of its initial activity even after 15 runs as reported by Chen et al [ 39 ].…”

Section: Resultscontrasting

confidence: 98%

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Covalent immobilization of β-galactosidase using a novel carrier alginate/tea waste: statistical optimization of beads modification and reusability

Abdella,

Hassan

2024

Bioprocess Biosyst Eng

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Abstractβ-galactosidase has been immobilized onto novel alginate/tea waste gel beads (Alg/TW) via covalent binding. Alg/TW beads were subjected to chemical modification through amination with polyethyleneimine (PEI) followed by activation with glutaraldehyde (GA). Chemical modification parameters including PEI concentration, PEI pH, and GA concentration were statistically optimized using Response Surface methodology (RSM) based on Box–Behnken Design (BBD). Analysis of variance (ANOVA) results confirmed the great significance of the model that had F value of 37.26 and P value < 0.05. Furthermore, the R2 value (0.9882), Adjusted R2 value (0.9617), and predicted R2 value (0.8130) referred to the high correlation between predicted and experimental values, demonstrating the fitness of the model. In addition, the coefficient of variation (CV) value was 2.90 that pointed to the accuracy of the experiments. The highest immobilization yield (IY) of β-galactosidase (75.1%) was given under optimized conditions of PEI concentration (4%), PEI pH (9.5), and GA concentration (2.5%). Alg/TW beads were characterized by FT-IR, TGA, and SEM techniques at each step of immobilization process. Moreover, the immobilized β-galactosidase revealed a very good reusability as it could be reused for 15 and 20 consecutive cycles keeping 99.7 and 72.1% of its initial activity, respectively. In conclusion, the environmental waste (tea waste) can be used in modern technological industries such as the food and pharmaceutical industry.

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Section: Resultscontrasting

confidence: 98%

“…The beads were washed after each cycle with 0.1 M phosphate buffer (pH 7.0) to remove the substrate residues and will be reused to initiate a new reaction cycle. The activity of immobilized enzyme in the 1st cycle was taken as 100% and the residual activity (Res A %) was determined using the following formula as suggested by [ 25 ] …”

Section: Methodsmentioning

confidence: 99%

Covalent immobilization of β-galactosidase using a novel carrier alginate/tea waste: statistical optimization of beads modification and reusability

Abdella,

Hassan

2024

Bioprocess Biosyst Eng

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“…The ΔG* values describe the spontaneity of the thermal deactivation processes, and higher values of ΔG* are evidence of the increased thermal stability of enzymes and show that thermal unfolding at high temperatures is controlled by the immobilization process. 49 A similar increase in ΔG* for α-amylase after immobilization has been observed in previous studies. 47,53 Moreover, the deactivation entropy (ΔS*) of the enzymes was estimated to be related to their thermal unfolding.…”

Section: ■ Results and Discussionsupporting

confidence: 87%

“…In another study, a half-life of 169 min was detected at 70 °C for α-amylase immobilized on glyoxyl agarose . The D -values of both enzymes were higher than those of a previously reported α-amylase immobilized on sugilite from modified basalt rock as a new carrier, which showed a D -value of 252.9 min at 60 °C …”

Section: Resultsmentioning

confidence: 72%

“…48 The D-values of both enzymes were higher than those of a previously reported α-amylase immobilized on sugilite from modified basalt rock as a new carrier, which showed a D-value of 252.9 min at 60 °C. 49 The deactivation energies (E d ) of free and immobilized PersiAmy2 and PersiAmy3 were determined from the slopes of the linear curves plotted between ln (k d ) and 1/T in the Supporting Information (Figure S4). The results showed that these values increased after immobilization compared to the free enzyme (Table 1).…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Computational Insights into the Selecting Mechanism of α-Amylase Immobilized on Cellulose Nanocrystals: Unveiling the Potential of α-Amylases Immobilized for Efficient Poultry Feed Hydrolysis

Motahar,

Tiyoula,

Motamedi

et al. 2023

Bioconjugate Chem.

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The selection of an appropriate amylase for hydrolysis poultry feed is crucial for achieving improved digestibility and high-quality feed. Cellulose nanocrystals (CNCs), which are known for their high surface area, provide an excellent platform for enzyme immobilization. Immobilization greatly enhances the operational stability of α-amylases and the efficiency of starch bioconversion in poultry feeds. In this study, we immobilized two metagenome-derived α-amylases, PersiAmy2 and PersiAmy3, on CNCs and employed computational methods to characterize and compare the degradation efficiencies of these enzymes for poultry feed hydrolysis. Experimental in vitro bioconversion assessments were performed to validate the computational outcomes. Molecular docking studies revealed the superior hydrolysis performance of PersiAmy3, which displayed stronger electrostatic interactions with CNCs. Experimental characterization demonstrated the improved performance of both α-amylases after immobilization at high temperatures (80 °C). A similar trend was observed under alkaline conditions, with α-amylase activity reaching 88% within a pH range of 8.0 to 9.0. Both immobilized α-amylases exhibited halotolerance at NaCl concentrations up to 3 M and retained over 50% of their initial activity after 13 use cycles. Notably, PersiAmy3 displayed more remarkable improvements than PersiAmy2 following immobilization, including a significant increase in activity from 65 to 80.73% at 80 °C, an increase in activity to 156.48% at a high salinity of 3 M NaCl, and a longer half-life, indicating greater thermal stability within the range of 60 to 80 °C. These findings were substantiated by the in vitro hydrolysis of poultry feed, where PersiAmy3 generated 53.53 g/L reducing sugars. This comprehensive comparison underscores the utility of computational methods as a faster and more efficient approach for selecting optimal enzymes for poultry feed hydrolysis, thereby providing valuable insights into enhancing feed digestibility and quality.

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Immobilization of Xylanase onto Starch Nanoparticles: A Reusable and Robust Nanobiocatalyst for Juice Clarification

Dik,

Bakar,

Ulu

et al. 2023

Starch Stärke

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Nanoparticles (NPs) have attracted interest recently as a promising support for the immobilization of enzymes.Xylanase (Xyl) has been utilized in the food industry for several purposes. To improve its stability and reusability,starch NPs (SNPs)are synthesized and assessed for Xyl immobilization for the first time. . The characterization results reveal that SNPs are successfully synthesized and Xyl@SNPs are effective as the immobilization carrier. The Xyl is immobilized on SNPs under optimized conditions leading to 91% immobilization efficiency. A shift in optimum pH (from 6.0 to 8.0) and temperature (from 70 to 60 °C) of Xyl is observed after immobilization. The Xyl@SNPs possess improve pH stability and thermal stability as well as operational stability. The Xyl@SNPs are easily reutilized and the residual activity is still higher than 62% after seven times. More importantly, the Xyl@SNPs have a lower Km value and enhance affinity for the substrate compared to the free Xyl. Additionally, the clarity of orange juice is increased by 76.0% by using Xyl@SNPs after 2 h incubation at 60 °C, pH 8.0. These positive results show promising support for the Xyl immobilization of SNPs, confirming that this immobilized enzyme‐based strategy is an effective technique for rapid clarification of targeted juices.

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Preparation and characterization of sugilite glass from basalt for α-amylase immobilization, statistical optimization of the immobilization process and description of free and immobilized enzyme

Cited by 14 publications

References 35 publications

Covalent immobilization of β-galactosidase using a novel carrier alginate/tea waste: statistical optimization of beads modification and reusability

Covalent immobilization of β-galactosidase using a novel carrier alginate/tea waste: statistical optimization of beads modification and reusability

Computational Insights into the Selecting Mechanism of α-Amylase Immobilized on Cellulose Nanocrystals: Unveiling the Potential of α-Amylases Immobilized for Efficient Poultry Feed Hydrolysis

Immobilization of Xylanase onto Starch Nanoparticles: A Reusable and Robust Nanobiocatalyst for Juice Clarification

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