Series-type enzyme deactivations: Influence of intermediate activity on deactivation kinetics

Henley, James P.; Sadana, Ajit

doi:10.1016/0141-0229(84)90076-0

Cited by 33 publications

(8 citation statements)

References 24 publications

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“…In fact an initial rise in activity has been reported for this preparation after treatment with H 2 O 2 at concentrations up to 6 M 15. Enzyme deactivation has been proposed to occur in several steps, with an intermediate being more active than the initial enzyme state 30. It seems that oxidation of amino acids is followed by further conformational changes before the enzyme becomes completely inactive.…”

Section: Resultsmentioning

confidence: 75%

Mass spectrometric analysis of peptides from an immobilized lipase: focus on oxidative modifications

Törnvall

Fürst

Hatti‐Kaul

et al. 2009

Rapid Comm Mass Spectrometry

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Liquid chromatography/tandem mass spectrometry (LC/MS/MS) was used to study the primary structure of immobilized Candida antarctica lipase B (Novozym(R)435) without detaching the enzyme from the carrier. The immobilized enzyme packed in a miniature column was subjected to proteolysis and the peptides released were injected into the mass spectrometer for analysis. The set-up was utilized to determine amino acid oxidation after treatment of the biocatalyst with hydrogen peroxide. In total, sequence coverage of more than 90% was obtained, containing almost all of the amino acids sensitive to oxidation. Oxidation of methionine, tryptophan and cystine residues was observed. The flow system also allowed evaluation of the enzyme activity prior to peptide analysis. The developed method is general and should be applicable to other immobilized enzyme systems and to different treatments.

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Section: Resultsmentioning

confidence: 75%

Mass spectrometric analysis of peptides from an immobilized lipase: focus on oxidative modifications

Törnvall

Fürst

Hatti‐Kaul

et al. 2009

Rapid Comm Mass Spectrometry

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“…The activity of rMnP‐yMVP was maintained at 94–105% of its initial activity in the 8‐hr testing period, suggesting the rMnP‐yMVP did not undergo an activity loss or inactivation at 25°C in 8 hr. The temperature‐induced inactivation of enzymes has been attributed to the enzymatic conformational changes, involving tertiary structure disorderings, such as breakage of disulfide bond and ionic interactions, and secondary structure disruption by breaking hydrogen bonds maintaining substructures (Henley & Sadana, , ). The enhancement of rMnP activity in yeast vaults is believed to be the result of constraint from vaults shells and surrounding rMnP enzyme molecules.…”

Section: Resultsmentioning

confidence: 99%

“…The temperature-induced inactivation of enzymes has been attributed to the enzymatic conformational changes, involving tertiary structure disorderings, such as breakage of disulfide bond and ionic interactions, and secondary structure disruption by breaking hydrogen bonds maintaining substructures (Henley & Sadana, 1984, 1985.…”

Section: Improved Stability and Catalytic Activities Of Mnp Packagementioning

confidence: 99%

Synthesis and assembly of human vault particles in yeast

Wang

Kickhoefer

Rome

et al. 2018

Biotech & Bioengineering

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Vault particles are the largest naturally occurring ribonucleoprotein complexes found in the cytoplasm. In all 78 copies of major vault protein (MVP) assemble on polyribosome templates, forming recombinant vault particles, which are of great interest as encapsulation carriers for therapeutics delivery and enzyme stabilization. Baculovirus-insect cell expression is the only system that has been developed for recombinant vault synthesis, but it has low scalability and slow production rate. In this study, we demonstrated the first use of yeast cells for the production of vault particles with full integrity and functionality solely by expressing the complementary DNA (cDNA) encoding MVP. Vaults synthesized in Pichia pastoris yeast cells are morphologically indistinguishable from recombinant vault particles produced in insect cells, and are able to package and stabilize enzymes resulting in improved longevity and catalytic efficiency. Thus, our results imply that the yeast system is an economical alternative to insect cells for the production of recombinant vaults. The consistency of vault morphology between yeast and insect cell systems also underlines that polyribosome templating may be conserved among eukaryotes, which promises the synthesis and assembly of recombinant human vault particles in other eukaryotic organisms.

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“…The specific activity and stability of this intermediate can be different from that of the native enzyme. For some enzymes, there was experimental evidence of different intermediate forms being created during the inactivation process (Henley & Sadana, 1984a), including peroxidase (the intermediates found differed from the native peroxidase by their molecular weight - Wang & Dimarco (1972) and by their electrophoretic mobility - Winter (1971)).…”

Section: Introductionmentioning

confidence: 99%

Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength

Saraiva

Oliveira

Lemos

et al. 1996

Int J of Food Sci Tech

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The thermal inactivation of horseradish peroxidase was studied in sodium phosphate buffer solutions and in pure water at pH 7 in the temperature range of 70–95°C. The sodium phosphate ions concentration affected both the thermostability and the kinetic patterns and had a stabilizing effect. The gradual change observed at low concentrations made a series‐type mechanism theoretically more coherent with the experimental observations than the conventionally applied two‐fraction model. In water the kinetics is apparently First order at high temperatures, while the results obtained at 25°C support the occurrence of a series‐type inactivation mechanism. The pH and enzyme concentration also affect the inactivation proFile, supporting the conclusion that the thermal inactivation is not a monomolecular process with respect to protein concentration.

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Series-type enzyme deactivations: Influence of intermediate activity on deactivation kinetics

Cited by 33 publications

References 24 publications

Mass spectrometric analysis of peptides from an immobilized lipase: focus on oxidative modifications

Mass spectrometric analysis of peptides from an immobilized lipase: focus on oxidative modifications

Synthesis and assembly of human vault particles in yeast

Analysis of the kinetic patterns of horseradish peroxidase thermal inactivation in sodium phosphate buffer solutions of different ionic strength

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