Co-evaluation of interaction parameters of genomic and plasmid DNA for a new chromatographic medium

Önal, Burcu; Acet, Ömür; Sanz, R.; Sanz-Pérez, Eloy S.; Erdönmez, Demet; Odabaşı, Mehmet

doi:10.1016/j.ijbiomac.2019.09.068

Cited by 16 publications

(4 citation statements)

References 40 publications

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“…In the literature, there is a wide application area of pHEMA based materials in different forms. It has found wide usage area not only in the biomedical field, but also as a solid support material in different fields of both environment and biochemistry [30][31][32][33][34].…”

Section: Introductionmentioning

confidence: 99%

Inhibition of bacterial adhesion by epigallocatechin gallate attached polymeric membranes

Acet

Dikici

Acet

et al. 2023

Colloids and Surfaces B: Biointerfaces

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Section: Introductionmentioning

confidence: 99%

Inhibition of bacterial adhesion by epigallocatechin gallate attached polymeric membranes

Acet

Dikici

Acet

et al. 2023

Colloids and Surfaces B: Biointerfaces

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“…[7] Affinity chromatography techniques take place wide implementations among all classic purification methods due to less purification steps. [8][9][10] Lately, immobilized metal affinity chromatography (IMAC) has been generally selected for the purification of biomolecules because of its excellent features such as low cost, high biomolecule adsorption capability, and great chemical stability. These characteristics are very important for large-ratio purification in industrial practises.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Alpha‐Amylase onto Ni²⁺ Attached Carbon Felt: Investigation of Kinetic Parameters from Potato Wastewater

et al. 2023

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Abstractα‐amylase is an important enzyme for textile, food, paper, and pharmaceutics industrial areas. In this study, Ni+2 attached carbon felt structures with nitrogen active site (Ni+2‐N‐ACF) were produced. The surface morphologies of the N‐ACF and Ni2+‐N‐ACF were investigated by means of SEM analysis. Ni2+ ions binding on the N‐ACFs were determined by energy dispersive X‐ray (EDX) analysis and a graphite furnace atomic absorption spectrometer (AAS). The effect of pH, ionic strength, initial α‐amylase concentration and temperature parameters were investigated for α‐amylase immobilization on Ni2+‐N‐ACF structures. In addition, pH and temperature effect on the activities of the free and the immobilized amylase, kinetic parameters, storage and operational stabilities were made decision. Lastly, starch degradation in potato waste water was tested on Ni2+‐N‐ACF. The obtained results showed that α‐amylase immobilized Ni2+‐N‐ACF can be used for starch degradation in industrial scale.This article is protected by copyright. All rights reserved

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“…Cryogels have 3D elastic interconnected macropores, spongy morphologies and good mechanical robustness [3]. They are extremely versatile tools when converted to desired purposes [4] such as purification/adsorption of biomolecules [5][6][7][8], and removal of some pollutants [9][10][11]. Increasing the existing properties while designing cryogels will further increase their potential use in different fields [4].…”

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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Co-evaluation of interaction parameters of genomic and plasmid DNA for a new chromatographic medium

Cited by 16 publications

References 40 publications

Inhibition of bacterial adhesion by epigallocatechin gallate attached polymeric membranes

Inhibition of bacterial adhesion by epigallocatechin gallate attached polymeric membranes

Immobilization of Alpha‐Amylase onto Ni²⁺ Attached Carbon Felt: Investigation of Kinetic Parameters from Potato Wastewater

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

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Co-evaluation of interaction parameters of genomic and plasmid DNA for a new chromatographic medium

Cited by 16 publications

References 40 publications

Inhibition of bacterial adhesion by epigallocatechin gallate attached polymeric membranes

Inhibition of bacterial adhesion by epigallocatechin gallate attached polymeric membranes

Immobilization of Alpha‐Amylase onto Ni2+ Attached Carbon Felt: Investigation of Kinetic Parameters from Potato Wastewater

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

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Immobilization of Alpha‐Amylase onto Ni²⁺ Attached Carbon Felt: Investigation of Kinetic Parameters from Potato Wastewater