Characteristics of Free vs. Immobilized Enzymes

Lartigue, Donald J.

doi:10.1016/b978-0-12-492350-8.50012-8

Immobilized Enzymes for Industrial Reactors 1975

DOI: 10.1016/b978-0-12-492350-8.50012-8

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Characteristics of Free vs. Immobilized Enzymes

Donald J. Lartigue¹

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1979

2023

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Cited by 4 publications

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Preparation and properties of immobilized flavokinase

Merrill¹,

McCormick²

1979

Biotech & Bioengineering

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Flavokinase (ATP: riboflavin 5'-phosphotransferase, EC 2.7.1.26) purified from rat liver by affinity chromatography, has been immobilized by amide linkage to omega-aminoalkyl-agarose beads. The immobilized enzyme differs from the soluble enzyme in having greater stability, slightly higher Km for the substrates, riboflavin and ATP, a broader pH optimum, and a lower energy of activation. These results suggest that the immobilized enzyme is influenced by the microenvironment of the bead and is subject to some degree of internal diffusional limitation. A small (3 ml), continuous, plug-flow reactor prepared with immobilized flavokinase effects 50% conversion of riboflavin to riboflavin 5'-phosphate (FMN) with a flow rate of 0.16 ml/min, which corresponds to an output of 5 nmol FMN/min. Immobilized flavokinase is effective for phosphorylating riboflavin and numerous riboflavin analogs and provides a facile method for preparing exclusively, unlike other synthetic methods, the 5'-phosphates.

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Preparation and properties of immobilized flavokinase

Merrill¹,

McCormick²

1979

Biotech & Bioengineering

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Biocatalytic synthesis, antimicrobial properties and toxicity studies of arginine derivative surfactants

et al. 2015

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Two novel arginine-based cationic surfactants were synthesized using as biocatalyst papain, an endopeptidase from Carica papaya latex, adsorbed onto polyamide. The classical substrate N (α)-benzoyl-arginine ethyl ester hydrochloride for the determination of cysteine and serine proteases activity was used as the arginine donor, whereas decyl- and dodecylamine were used as nucleophiles for the condensation reaction. Yields higher than 90 and 80 % were achieved for the synthesis of N (α)-benzoyl-arginine decyl amide (Bz-Arg-NHC10) and N (α)-benzoyl-arginine dodecyl amide (Bz-Arg-NHC12), respectively. The purification process was developed in order to make it more sustainable, by using water and ethanol as the main separation solvents in a single cationic exchange chromatographic separation step. Bz-Arg-NHC10 and Bz-Arg-NHC12 proved antimicrobial activity against both Gram-positive and Gram-negative bacteria, revealing their potential use as effective disinfectants as they reduced 99 % the initial bacterial population after only 1 h of contact. The cytotoxic effect towards different cell types of both arginine derivatives was also measured. Bz-Arg-NHCn demonstrated lower haemolytic activity and were less eye-irritating than the commercial cationic surfactant cetrimide. A similar trend could also be observed when cytotoxicity was tested on hepatocytes and fibroblast cell lines: both arginine derivatives were less toxic than cetrimide. All these properties would make the two novel arginine compounds a promising alternative to commercial cationic surfactants, especially for their use as additives in topical formulations.

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Amperometric bienzymatic biosensor in flow injection analysis system for determination of aspartame in foods

Tangtawewipat,

Thanachasai

2023

Food Sci Biotechnol

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Characteristics of Free vs. Immobilized Enzymes

Cited by 4 publications

References 19 publications

Preparation and properties of immobilized flavokinase

Preparation and properties of immobilized flavokinase

Biocatalytic synthesis, antimicrobial properties and toxicity studies of arginine derivative surfactants

Amperometric bienzymatic biosensor in flow injection analysis system for determination of aspartame in foods

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