l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters

Noma, Samir Abbas Ali; Acet, Ömür; Ulu, Ahmet; Önal, Burcu; Odabaşı, Mehmet; Ateş, Burhan

doi:10.1016/j.polymertesting.2020.106980

Cited by 23 publications

(9 citation statements)

References 48 publications

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“…Additionally, pectinase preparation@ZSM-5(85) possessed a higher V max than the other forms of pectinase preparation@ZSM-5 and free pectinase preparation, and its enzyme activity was 83% higher than that of free pectinase preparation. Immobilized enzymes had higher V max values than those of the free enzymes, and an increase in V max could be due to the activation of their catalytic active centers because of a change in the enzyme conformation caused by immobilization ( Ali Noma et al, 2021 ), which increased the substrate-to-product conversion rate.…”

Section: Resultsmentioning

confidence: 99%

Immobilized Crosslinked Pectinase Preparation on Porous ZSM-5 Zeolites as Reusable Biocatalysts for Ultra-Efficient Hydrolysis of β-Glycosidic Bonds

et al. 2021

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In this study, we immobilized pectinase preparation on porous zeolite ZSM-5 as an enzyme carrier. We realized this immobilized enzyme catalyst, pectinase preparation@ZSM-5, via a simple combined strategy involving the van der Waals adsorption of pectinase preparation followed by crosslinking of the adsorbed pectinase preparation with glutaraldehyde over ZSM-5. Conformal pectinase preparation coverage of various ZSM-5 supports was achieved for the as-prepared pectinase preparation@ZSM-5. The porous pectinase preparation@ZSM-5 catalyst exhibited ultra-efficient biocatalytic activity for hydrolyzing the β-glycosidic bonds in the model substrate 4-nitrophenyl β-D-glucopyranoside, with a broad operating temperature range, high thermal stability, and excellent reusability. The relative activity of pectinase preparation@ZSM-5 at a high temperature (70 °C) was nine times higher than that of free pectinase preparation. Using thermal inactivation kinetic analysis based on the Arrhenius law, pectinase preparation@ZSM-5 showed higher activation energy for denaturation (315 kJ mol−1) and a longer half-life (62 min−1) than free pectinase preparation. Moreover, a Michaelis–Menten enzyme kinetic analysis indicated a higher maximal reaction velocity for pectinase preparation@ZSM-5 (0.22 µmol mg−1 min−1). This enhanced reactivity was attributed to the microstructure of the immobilized pectinase preparation@ZSM-5, which offered a heterogeneous reaction system that decreased the substrate–pectinase preparation binding affinity and modulated the kinetic characteristics of the enzyme. Additionally, pectinase preparation@ZSM-5 showed the best ethanol tolerance among all the reported pectinase preparation-immobilized catalysts, and an activity 247% higher than that of free pectinase preparation at a 10% (v/v) ethanol concentration was measured. Furthermore, pectinase preparation@ZSM-5 exhibited potential for practical engineering applications, promoting the hydrolysis of β-glycosidic bonds in baicalin to convert it into baicalein. This was achieved with a 98% conversion rate, i.e., 320% higher than that of the free enzyme.

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Section: Resultsmentioning

confidence: 99%

Immobilized Crosslinked Pectinase Preparation on Porous ZSM-5 Zeolites as Reusable Biocatalysts for Ultra-Efficient Hydrolysis of β-Glycosidic Bonds

et al. 2021

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“…C-H stretching stretching stretching band was monitored at 2950/cm. In addition, a peak at 1717/cm of the stretching vibration of the C=O group was determined in the HEMA and GMA ester [1,27]. After enzyme immobilization, the FTIR spectrum of the hybrid cryogel showed two new peaks at around 1550/cm and 1660/cm.…”

Section: Characterization Studiesmentioning

confidence: 97%

“…Cryogels are biomaterials that are in a subcategory of hydrogels and have perfect physical features [1,2]. Cryogels have 3D elastic interconnected macropores, spongy morphologies and good mechanical robustness [3].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of xylanase enzyme on poly-(HEMA-co-GMA) cryogel

Noma

2022

MANAS Journal of Engineering

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In this study, a polyethyleneimine (PEI) coated poly-(HEMA-co-GMA), hybrid cryogel column (HCC), was designed. HCC was synthesized via polymerization of gel-former factors at minus temperatures. The characterization experiments of the HCC were conducted through SEM, and FTIR experiments. At the end of the experimental periods, there was no significant decrease in the performance of the HCC. Then the HCC was used as a novel support for xylanase immobilization for the first time. the successful immobilization of xylanase was confirmed by FT-IR, while the biochemical properties and stability of the PHG/PI-Xyl were evaluated in terms of optimum pH, optimum temperature, thermostability, storage stability, reusability, and kinetic parameters, The optimum activities for both free and immobilized enzyme were recorded at pH 6.0, while optimum temperature for free was 55 °C and for PHG/PI-Xyl 60 °C. The PHG/PI-Xyl displayed remarkable thermal stability for 180 min at 60 °C, with 53.55%, and for free Xyl 32.05%. Meanwhile, it retained up to 49% and 69 % for free and immobilized xylanase of original activities after 4 weeks of storage at room temperature. The PHG/PI-Xyl retained about 58% of its original activity after 10 consecutive reuses, while Km for the free Xyl and PHG/PI-Xyl were calculated at 4.05 mg/mL and 2.62 mg/mL, whereas Vmax133.33 U/mL and 188.68 U/mL, respectively. As envisioned, this study suggests a promising way to solve the problems of high price and poor operational stability of the enzyme during biocatalytic.

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“…18,[67][68][69][70][71][72] At the same time, researchers are not only exploring possible sources of production, but also experimenting with different immobilization methods to enhance therapeutic efficacy, such as the novel p(HEMA-GMA) cryogel invented by Noma et al which resulted in a significant increase in enzyme activity and stability, and Ca-ALG/MWCNT-COOH hybrid beads designed by Ulu et al which enhanced the affinity of the enzyme for the substrate. [73][74][75] 4. Activity assay L-ASNase alleviates ALL by depleting L-Asn in leukemia cells and exerting a cytotoxic effect on these cells.…”

Section: Rsc Medicinal Chemistry Reviewmentioning

confidence: 99%

Overview of the structure, side effects, and activity assays of l-asparaginase as a therapy drug of acute lymphoblastic leukemia

Wang

et al. 2022

RSC Med. Chem.

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l-asparaginase immobilized p(HEMA-GMA) cryogels: A recent study for biochemical, thermodynamic and kinetic parameters

Cited by 23 publications

References 48 publications

Immobilized Crosslinked Pectinase Preparation on Porous ZSM-5 Zeolites as Reusable Biocatalysts for Ultra-Efficient Hydrolysis of β-Glycosidic Bonds

Immobilized Crosslinked Pectinase Preparation on Porous ZSM-5 Zeolites as Reusable Biocatalysts for Ultra-Efficient Hydrolysis of β-Glycosidic Bonds

Immobilization of xylanase enzyme on poly-(HEMA-co-GMA) cryogel

Overview of the structure, side effects, and activity assays of l-asparaginase as a therapy drug of acute lymphoblastic leukemia

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