Active and intelligent packaging for food: is it the future?

This paper gives an overview of the legal consequences of a new EU framework regulation on food contact materials which includes controls on active and intelligent packaging. Recent developments in active and intelligent packaging systems are described, two examples of which aim at achieving improvements in quality and safety of food products. The first one is an on-command preservative-releasing packaging system.

Horseradish peroxidase-catalyzed cross-linking of feruloylated arabinoxylans with beta-casein.

Heterologous conjugates of wheat arabinoxylan and beta-casein were prepared via enzymatic cross-linking, using sequential addition of the arabinoxylan to a mixture of beta-casein, peroxidase, and hydrogen peroxide. The maximal formation of adducts between the beta-casein and the feruloylated arabinoxylan was reached at a protein-to-arabinoxylan ratio of 10:1, in combination with a molar ratio hydrogen peroxide to substrate of 2:1 and a molar protein-to-enzyme ratio between 10(2) and 10(4). The protein-arabinoxylan adducts were separated from the arabinoxylan homopolymers by size exclusion and anion exchange chromatography.

Purification and substrate specificity of transglutaminases from blood and Streptoverticillium mobaraense.

A procedure for a fast and simple purification of bovine plasma transglutaminase was developed, which resulted in a homogeneous enzyme preparation. Two different procedures were developed for the purification of pig erythrocyte transglutaminase, both of which resulted in partial purification. Both enzymes were used in cross-linking reactions of alpha-lactalbumin, beta-lactoglobulin, bovine serum albumin, casein, hemoglobin, glycinin, and myosin.

Functional complementation analysis of yeast bc1 mutants. A study of the mitochondrial import of heterologous and hybrid proteins.

Previous complementation studies with yeast bc1 mutants, defective in subunit VII or VIII, using heterologous and hybrid subunits, suggested that the requirement for import into mitochondria might significantly restrict the scope of this test for compatible proteins. Prediction algorithms indicate that the N-terminal domain of subunit VII contains all known characteristics of a mitochondrial targeting signal, whereas in subunit VIII such a signal is absent from the N-terminal domain, but possibly present in an internal region of the protein. Despite the fact that the characteristics of a mitochondrial import signal are found in the N-terminus of all known subunit-VII orthologues, in vitro import experiments show that the protein of human origin is not imported into yeast mitochondria.

Metabolic control analysis of the bc1 complex of Saccharomyces cerevisiae: effect on cytochrome c oxidase, respiration and growth rate.

A number of strains varying in steady-state level of assembled bc1 complex were used to test the conclusions from inhibitor titration experiments with isolated mitochondria that, in cells of Saccharomyces cerevisiae grown on non-fermentable carbon sources, the control coefficient of the bc1 complex on the mitochondrial respiratory capacity equals 1 and the respiratory chain consists of supermolecular respiratory units [Boumans, Grivell and Berden (1998) J. Biol. Chem.

The respiratory chain in yeast behaves as a single functional unit.

Inhibitor titrations using antimycin have been used to study the pool behavior of ubiquinone and cytochrome c in the respiratory chain of the yeast Saccharomyces cerevisiae. If present in a homogeneous pool, these carriers should be able to diffuse freely through or along the membrane respectively and accept and subsequently donate electrons to an infinite number of the respective respiratory complex. However, we show that under physiological conditions neither ubiquinone nor cytochrome c exhibits pool behavior, implying that the respiratory chain in yeast is one functional unit.

The role of subunit VIII in the structural stability of the bc1 complex from Saccharomyces cerevisiae studied using hybrid complexes.

The QCR8 genes encoding subunit VIII of the bc1 complex from Kluyveromyces lactis and Schizosaccharomyces pombe partially complement the respiratory-deficient phenotype of a S. cerevisiae QCR8-null mutant. This implies that the heterologous Qcr8 subunits can be imported by S.

Differential inhibition of the yeast bc1 complex by phenanthrolines and ferroin. Implications for structure and catalytic mechanism.

o-Phenanthroline and m-phenanthroline both inhibit the electron transfer activity of lauryl maltoside-solubilized yeast bc1 complex progressively with time. Pre-steady-state kinetics indicate that these compounds bind to the complex on the intermembrane space side, thereby blocking reduction of cytochrome b via the ubiquinol oxidation site. o-Phenanthroline is additionally capable of chelating an iron atom derived from the Rieske Fe-S cluster, thereby distorting the structure of the Rieske protein.

Topological organization of subunits VII and VIII in the ubiquinol-cytochrome c oxidoreductase of Saccharomyces cerevisiae.

To determine the topology of subunit VIII of the yeast ubiquinol-cytochrome c oxidoreductase in the mitochondrial inner membrane, an epitope has been introduced in the N-terminal half of this protein. Previous topology studies had shown that at least the C-terminus faces the intermembrane space [Hemrika and Berden (1990) Eur. J.

Identification of additional homologues of subunits VII and VIII of the ubiquinol-cytochrome c oxidoreductase enables definition of consensus sequences.

The Candida utilis QCR7 gene encoding subunit VII of the ubiquinol-cytochrome c oxidoreductase was isolated by functional complementation of the Saccharomyces cerevisiae subunit VII-null mutant. Several other subunit VII homologues as well as homologues for subunit VIII were identified by screening the GenBank database. Some of these homologues for subunit VII could only be identified as such using a consensus sequence that was derived from the multiple sequence alignment.

cDNA sequence of subunit VIII of ubiquinol-cytochrome-c oxidoreductase from Schizosaccharomyces pombe.

We have cloned a cDNA coding for subunit VIII of the ubiquinol-cytochrome-c oxidoreductase of Schizosaccharomyces pombe by functional complementation of the null mutant in the QCR8 gene of Saccharomyces cerevisiae. DNA sequence analysis reveals an open-reading frame of 276 bp encoding a 10.5 kDa protein with 51% amino acid sequence identity to its counterpart in S.

Site-directed mutagenesis of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Binding of the peripheral components E1p and E3.

Site-directed mutagenesis was performed in the protease-sensitive region, between the lipoyl and catalytic domains and in the catalytic domain, of the dihydrolipoyl transacetylase component (E2p) of the pyruvate dehydrogenase complex from Azotobacter vinelandii. The interaction of the mutated enzymes with the peripheral components pyruvate dehydrogenase (E1p) and lipoamide dehydrogenase (E3) was studied by gel filtration experiments, analytical ultracentrifugation and reconstitution of the pyruvate dehydrogenase complex. Upon binding of peripheral components, the 24-subunit core of A.