Preparation and characterisation of ribonuclease monolithic bioreactor

Benčina, Mojca; Babič, Janja; Podgornik, Aleš

doi:10.1016/j.chroma.2006.12.083

Cited by 28 publications

(23 citation statements)

References 27 publications

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“…The Michaelis–Menten constants determined for conversion of pyruvate to L‐lactate by free and bound lactate dehydrogenase were measured to be equal to 0.44 and 0.54 mM, respectively. The comparable result was established for ribonuclease A (RNase) immobilized on CIM disk by Benčina et al , He et al for choline oxidase immobilized on silica microcolumn and Kato et al for trypsin encapsulated into sol‐gel silica monolith . Particularly, K M for free and bound RNase in the reaction of cytidine‐(2′)3′‐cyclic monophosphate hydrolysis appeared to be 0.52 for free and 0.62 mM for immobilized enzyme, whereas for free and bound choline oxidase in the reaction of oxidation of cholin into choline acetate, these values were 2.1 and 1.7 mM, respectively.…”

Section: Kinetics Of Enzymatic Reactionsupporting

confidence: 67%

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Влах

Tennikova

2013

J of Separation Science

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In the last decade, the application of monolithic materials has rapidly expanded to the realization of flow-through bioconversion processes. Up to these days, different classes of enzymes such as hydrolases, lyases, and oxidoreductases have been immobilized on organic, inorganic, or hybrid monolithic materials to prepare the effective flow-through enzymes reactors for application in proteomics, biotechnology, pharmaceutics, organic synthesis, and biosensoring. Current review describes the results of kinetic study and specialties of flow-through immobilized enzyme reactors based on the existing monolithic materials.

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Section: Kinetics Of Enzymatic Reactionsupporting

confidence: 67%

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Влах

Tennikova

2013

J of Separation Science

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“…CDI is a zero-length cross-linker, which activates carboxylic acids and hydroxyl groups to an intermediate that is reactive to nucleophiles, and considerably more stable than water soluble carbodiimide cross-linkers, thus allowing longer conjugation times in aqueous environments. Although it is widely used in peptide synthesis, biomolecule labeling, and immobilization of proteins onto organic and inorganic solid supports [41, 48–50], direct linkage of DNA to silicon substrates by CDI activation is an emerging bioconjugation technique. This chemistry could be particularly useful in the fields of label-free biosensing, in which highest device sensitivities are achieved when the biorecognition event occurs in close proximity to the sensing surface.…”

Section: Resultsmentioning

confidence: 99%

Bioconjugation techniques for microfluidic biosensors

Goddard

Erickson

2009

Anal Bioanal Chem

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We have evaluated five bioconjugation chemistries for immobilizing DNA onto silicon substrates for microfluidic biosensing applications. Conjugation by organosilanes is compared with linkage by carbonyldiimidazole (CDI) activation of silanol groups and utilization of dendrimers. Chemistries were compared in terms of immobilization and hybridization density, stability under microfluidic flow-induced shear stress, and stability after extended storage in aqueous solutions. Conjugation by dendrimer tether provided the greatest hybridization efficiency; however, conjugation by aminosilane treated with glutaraldehyde yielded the greatest immobilization and hybridization densities, as well as enhanced stability to both shear stress and extended storage in an aqueous environment. Direct linkage by CDI activation provided sufficient immobilization and hybridization density and represents a novel DNA bioconjugation strategy. Although these chemistries were evaluated for use in microfluidic biosensors, the results provide meaningful insight to a number of nanobiotechnology applications for which microfluidic devices require surface biofunctionalization, for example vascular prostheses and implanted devices.

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“…Besides, microbial RNases have higher potential owing to different enzymatic characteristics such as thermostability and alkaliphility (Voss et al 2006). Bencina et al (2007) have demonstrated that immobilized RNase A can be used for RNA removal in plasmid DNA preparation without an additional step for the purification of the enzyme. Moreover, they also have shown that the enzyme exhibited maximum activity in the presence of a broad range of NaCl.…”

Section: Purification Of Plasmid Dna For Dna Vaccine and Gene Therapymentioning

confidence: 99%

Microbial ribonucleases (RNases): production and application potential

Hameş

Demir

2015

World J Microbiol Biotechnol

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Ribonuclease (RNase) is hydrolytic enzyme that catalyzes the cleavage of phosphodiester bonds in RNA. RNases play an important role in the metabolism of cellular RNAs, such as mRNA and rRNA or tRNA maturation. Besides their cellular roles, RNases possess biological activity, cell stimulating properties, cytotoxicity and genotoxicity. Cytotoxic effect of particular microbial RNases was comparable to that of animal derived counterparts. In this respect, microbial RNases have a therapeutic potential as anti-tumor drugs. The significant development of DNA vaccines and the progress of gene therapy trials increased the need for RNases in downstream processes. In addition, RNases are used in different fields, such as food industry for single cell protein preparations, and in some molecular biological studies for the synthesis of specific nucleotides, identifying RNA metabolism and the relationship between protein structure and function. In some cases, the use of bovine or other animal-derived RNases have increased the difficulties due to the safety and regulatory issues. Microbial RNases have promising potential mainly for pharmaceutical purposes as well as downstream processing. Therefore, an effort has been given to determination of optimum fermentation conditions to maximize RNase production from different bacterial and fungal producers. Also immobilization or strain development experiments have been carried out.

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Preparation and characterisation of ribonuclease monolithic bioreactor

Cited by 28 publications

References 27 publications

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Flow‐through immobilized enzyme reactors based on monoliths: II. Kinetics study and application

Bioconjugation techniques for microfluidic biosensors

Microbial ribonucleases (RNases): production and application potential

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