Parsley plastocyanin. The possible presence of sulfhydryl and tyrosine in the copper environment.

The retention of biologically available vitamin B6 during storage was examined using dehydrated food systems fortified with various B6 vitamers. Storage conditions of 37°C and 0.6 water activity (aw) were selected to permit estimation of maximum rates of nonenzymatic browning and vitamin degradation typically encountered in food storage. The stability of the vitamers during storage was evaluated by periodic assay with a high performance liquid chromatographic (HPLC) method. Losses of pyridoxine (PN), pyridoxamine (PM), pyridoxal (PL), and pyridoxal phosphate (PLP) could be described by fist order kinetics. When stored in small volume metal containers, the first order rate constants were 0.015–0.020 day−1 for PL, PM and PLP, and 0.0049 day−1 for PN degradation in food systems. Storage in metal cans which provided a large headspace volume resulted in significantly lower rates of browning and degradation of the B6 vitamers. The only significant degradation mechanism identified was the binding of PLP to proteins to form e-pyridoxyllysine. Correlation of rat bioassay results with microbiological and HPLC assay data indicated that the B6 vitamers remaining after storage for 128 days at 37°C retained full vitamin activity. Determination of the model system vitamin B6 content by the semiautomated fluorometric procedure yielded consistently high results, as found in previous research. These studies indicate that HLPC and microbiological assay results accurately reflect the content of biologically available vitamin B6 in dehydrated food systems after storage at 37°C and 0.6 aw for 128 days. They also demonstrate the potential for application of the HPLC assay to the determination of vitamin B6 in foods.

Assessment of storage effects on vitamin b6 stability and bioavailability in dehydrated food systems

Amine oxidases (AO) are enzymes widely distributed among all living organisms.1 Their widespread occurrence accounts for an undoubtedly relevant biological function in biogenic amine metabolism. AOs represent a class of enzymes heterogenous in structure, catalytic mechanism and mode of substrate oxidation. Mono-, di- and polyamines, as well as several N-acyl amines, are oxidatively deaminated by AOs in a reaction consuming O2 and H2O and producing the corresponding aldehyde, the removed amine moiety and H2O2 in stoichiometric amounts according to the following equations: 

$${\text{R - C}}{{\text{H}}_{\text{2}}}{\text{ - N}}{{\text{H}}_{\text{2}}}{\text{ + }}{{\text{O}}_{\text{2}}}{\text{ + }}{{\text{H}}_{\text{2}}}{\text{O }} \to {\text{R - CHO + N}}{{\text{H}}_{\text{3}}}{\text{ + }}{{\text{H}}_{\text{2}}}{{\text{O}}_{\text{2}}}$$

cleavage at a primary amino group (terminal oxidation reaction).

The biological functions of amine oxidases and their reaction products: an overview.

Prediction of the amount and rate of histamine degradation by diamine oxidase (DAO)

Further properties of the polyamine oxidase from oat seedlings

The alkaline bleaching of Pseudomonas fluorescens azurin.

Salt effect on diamine oxidase activity.

Oxidation of a lysine-copper-pyridoxal phosphate complex.

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The alkaline bleaching of Pseudomonas fluorescens azurin.

Salt effect on diamine oxidase activity.

Oxidation of a lysine-copper-pyridoxal phosphate complex.