Biomedical subjects

I Van den Broeck

Publications and source records attributed to I Van den Broeck.

8 recordsLinked to original sources

PubMed2000

Inactivation of orange pectinesterase by combined high-pressure and -temperature treatments: a kinetic study.

Pressure and/or temperature inactivation of orange pectinesterase (PE) was investigated. Thermal inactivation showed a biphasic behavior, indicating the presence of labile and stable fractions of the enzyme. In a first part, the inactivation of the labile fraction was studied in detail. The combined pressure-temperature inactivation of the labile fraction was studied in the pressure range 0.1-900 MPa combined with temperatures from 15 to 65 degrees C. Inactivation in the pressure-temperature domain specified could be accurately described by a first-order fractional conversion model, estimating the inactivation rate constant of the labile fraction and the remaining activity of the stable fraction. Pressure and temperature dependence of the inactivation rate constants of the labile fraction was quantified using the Eyring and Arrhenius relations, respectively. By replacing in the latter equation the pressure-dependent parameters (E(a), k(ref)(T)()) by mathematical expressions, a global model was formulated. This mathematical model could accurately predict the inactivation rate constant of the labile fraction of orange PE as a function of pressure and temperature. In a second part, the stable fraction was studied in more detail. The stable fraction inactivated at temperatures exceeding 75 degrees C. Acidification (pH 3.7) enhanced thermal inactivation of the stable fraction, whereas addition of Ca(2+) ions (1 M) suppressed inactivation. At elevated pressure (up to 900 MPa), an antagonistic effect of pressure and temperature on the inactivation of the stable fraction was observed. The antagonistic effect was more pronounced in the presence of a 1 M CaCl(2) solution as compared to the inactivation in water, whereas it was less pronounced for the inactivation in acid medium.

Carboxylic Ester Hydrolases↗

PubMed1999

Thermal and combined pressure--temperature inactivation of orange pectinesterase: influence of pH and additives.

Inactivation of commercially available orange pectinesterase (PE) was investigated under isothermal and isothermal-isobaric conditions. In both cases, inactivation data could be accurately described by a fractional conversion model. The influence of enzyme concentration, pH, Ca(2+) concentration, and sucrose on the inactivation kinetics was studied. Enzyme stability against heat and pressure increased by increasing enzyme concentration. An increased Ca(2+) concentration caused sensitization to temperature and increased the residual fraction active PE after thermal treatment. To the contrary, in the case of pressure treatment, decreasing Ca(2+) concentrations increased pressure inactivation. The remaining fraction active PE after pressure treatment was not influenced by the addition of Ca(2+) ions. Acidification accelerated thermal as well as pressure-temperature inactivation, whereas in the presence of sucrose an increased temperature and pressure stability of orange PE was observed. Sucrose had no influence on the remaining activity after thermal treatment, but it increased the residual fraction after pressure treatment. The remaining fraction was for all additives studied independent of the pressure and temperature level applied except for the inactivation in an acid medium, when a decrease of the residual fraction was observed with increasing temperature and pressure.

Carboxylic Ester Hydrolases↗

PubMed1999

Influence of pH, benzoic acid, glutathione, EDTA, 4-hexylresorcinol, and sodium chloride on the pressure inactivation kinetics of mushroom polyphenol oxidase.

Pressure inactivation of mushroom PPO was studied for pH values ranging from 4 to 8, and the effect of some antibrowning agents on the pressure stability of mushroom PPO at pH 6.5 was evaluated. pH reduction below 6.5 resulted in a lowered inactivation threshold pressure and an increase of the absolute value of the activation volume (or a decrease of the z(p) value), the latter two parameters reflecting the pressure dependency of the inactivation rate constant. An increase in pH from 6.5 to 8, on the other hand, did only marginally affect the pressure stability of the enzyme. Mushroom PPO at pH 6.5 was markedly sensitized toward pressure by the presence of 2.5 mM 4-hexylresorcinol and slightly stabilized by the presence of 5 mM EDTA. The presence of 5 mM glutathione, sodium chloride, or benzoic acid caused no significant alteration of the enzyme pressure stability. Only in the presence of 4-hexylresorcinol, significant changes of the activation volume and z(p) value were noticed.

Agaricales↗

PubMed1998

Kinetics of combined pressure-temperature inactivation of avocado polyphenoloxidase.

Irreversible combined pressure-temperature inactivation of the food quality related enzyme polyphenoloxidase was investigated. Inactivation rate constants (k) were obtained for about one hundred combinations of constant pressure (0.1-900 MPa) and temperature (25-77.5 degrees C). According to the Eyring and Arrhenius equation, activation volumes and activation energies, respectively, representing pressure and temperature dependence of the inactivation rate constant, were calculated for all temperatures and pressures studied. In this way, temperature and pressure dependence of activation volume and activation energy, respectively, could be considered. Moreover, for the first time, a mathematical model describing the inactivation rate constant of a food quality-related enzyme as a function of pressure and temperature is formulated. Such pressure-temperature inactivation models for food quality-related aspects (e.g., the spoilage enzyme polyphenoloxidase) form the engineering basis for design, evaluation, and optimization of new preservation processes based on the combined effect of temperature and pressure. Furthermore, the generated methodology can be used to develop analogous kinetic models for microbiological aspects, which are needed from a safety and legislative point of view, and other quality aspects, e.g., nutritional factors, with a view of optimal quality and consumer acceptance.

Catechol Oxidase↗

PubMed1995

Evolution according to large ribosomal subunit RNA.

Evolutionary trees were constructed, by distance methods, from an alignment of 225 complete large subunit (LSU) rRNA sequences, representing Eucarya, Archaea, Bacteria, plastids, and mitochondria. A comparison was made with trees based on sets of small subunit (SSU) rRNA sequences. Trees constructed on the set of 172 species and organelles for which the sequences of both molecules are known had a very similar topology, at least with respect to the divergence order of large taxa such as the eukaryotic kingdoms and the bacterial divisions. However, since there are more than ten times as many SSU as LSU rRNA sequences, it is possible to select many SSU rRNA sequence sets of equivalent size but different species composition. The topologies of these trees showed considerable differences according to the particular species set selected. The effect of the dataset and of different distance correction methods on tree topology was tested for both LSU and SSU rRNA by repetitive random sampling of a single species from each large taxon. The impact of the species set on the topology of the resulting consensus trees is much lower using LSU than using SSU rRNA. This might imply that LSU rRNA is a better molecule for studying wide-range relationships. The mitochondria behave clearly as a monophyletic group, clustering with the Proteobacteria. Gram-positive bacteria appear as two distinct groups, which are found clustered together in very few cases. Archaea behave as if monophyletic in most cases, but with a low confidence.

Animal Population Groups↗

PubMed1995

The phylogeny of the Hyphochytriomycota as deduced from ribosomal RNA sequences of Hyphochytrium catenoides.

Based on biochemical and ultrastructural data, hyphochytriomycetes are believed to share an ancestor with oomycetes and heterokont algae. In order to study the phylogeny of the hyphochytriomycetes, we determined both the small- and large-subunit ribosomal RNA sequence of Hyphochytrium catenoides. Phylogenetic trees were constructed using the neighbor-joining and maximum-parsimony method and include representatives of Chlorobionta, Fungi, Metazoa, Alveolata, and all known Heterokonta. Our main conclusion is that the hyphochytriomycetes form a monophyletic group with the oomycetes and heterokont algae and that they are probably the closest relatives of the oomycetes. However, the order of divergence between the various heterokont algal phyla and the oomycete-hyphochytriomycete cluster remains uncertain.

Base Sequence↗

PubMed1994

Database on the structure of small ribosomal subunit RNA.

The database on small ribosomal subunit RNA structure contains (June 1994) 2824 nucleotide sequences. All these sequences are stored in the form of an alignment based on the adopted secondary structure model, which in turn is corroborated by the observation of compensating substitutions in the alignment. The complete database is made available to the scientific community through anonymous ftp on our server in Antwerp. A special effort was made to improve electronic retrieval and a program is supplied that allows to create different file formats. The database can also be obtained from the EMBL nucleotide sequence library.

Animals↗

PubMedDate not supplied

Influence of pH, benzoic acid, EDTA, and glutathione on the pressure and/or temperature inactivation kinetics of mushroom polyphenoloxidase.

The pressure and/or temperature inactivation of mushroom polyphenoloxidase (PPO) in the absence and presence of EDTA, benzoic acid, and glutathione was studied on a kinetic basis. In addition, the effect of pH was evaluated. The temperature stability of PPO at atmospheric pressure increased with increasing pH up to pH 6.5. The pressure stability of PPO at room temperature (25 degrees C) also increased with increasing pH. EDTA slightly increased the thermal stability of the enzyme but did not alter the pressure stability of PPO. Benzoic acid protected the enzyme toward temperature but caused sensitization toward pressure when used at a concentration of 50 mM. Glutathione produced sensitization to both temperature and pressure. It is suggested that the sensitizing effect of glutathione is due to an interaction with a disulfide bond of the enzyme.

Basidiomycota↗