Change in α‐tocopherol contents,lipid oxidation and fatty acid profile in eggs enriched with linolenic acid or very long‐chain ω3 polyunsaturated fatty acids after different processing methods

The influences of dietary supplementation with α‐tocopheryl acetate (α‐TA) and of processing (by hard‐boiling and scrambling) of eggs enriched with ω3 fatty acids, either very long‐chain ω3 polyunsaturated fatty acids (VLC ω3 PUFAs) or linolenic acid (LNA), on fatty acid composition, α‐tocopherol content and lipid oxidation (thiobarbituric acid (TBA) values) were studied. Four dietary treatments were formulated from a basal diet containing 40 g kg^?1 linseed oil (LO) or fish oil (FO) combined with either 0 or 100 mg α‐TA kg^?1 of feed. Eggs from LO treatments were enriched with LNA and those from FO treatments were rich in VLC ω3 PUFAs. Neither processing nor dietary supplementation with α‐TA modified greatly the fatty acid profile of eggs. Dietary supplementation with α‐TA increased the α‐tocopherol content of eggs (187.2 versus 407.9 µg g^?1 dry matter). Eggs from FO treatments showed lower α‐tocopherol content than those from LO treatments (273.5 versus 321.6 µg g^?1 dry matter), and processing of eggs enriched with VLC ω3 PUFA reduced the α‐tocopherol content by a significant 16%. Moreover, processing of eggs increased lipid oxidation two‐ to nine‐fold. Oxidation levels of hard‐boiled eggs were 30.4% higher than those of scrambled eggs. TBA values in hard‐boiled and scrambled eggs were significantly reduced when 100 mg α‐TA kg^?1 of feed supplemented the diet only in those eggs enriched with VLC ω3 PUFA (from FO treatments). Copyright © 2003 Society of Chemical Industry     

Isolation of obligate anaerobic rumen bacteria capable of degrading the neurotoxin β‐ODAP (β‐N‐oxalyl‐L‐α,β‐diaminopropionic acid) as evaluated by a liquid chromatography/biosensor analysis system

Six pure strains of obligate anaerobes capable of degrading the toxin β‐N‐oxalyl‐L ‐α, β‐diaminopropionic acid (β‐ODAP) contained in grass pea (Lathyrus sativus) have been isolated from cow rumen. The new isolates were identified as Megasphaera elsdenii (five different genotypes) and Clostridium bifermentans using 16S rDNA analysis. The β‐ODAP degrading efficiency of the isolates was evaluated by measuring the amount of β‐ODAP in the growth medium, which contained β‐ODAP as the only carbon source, before and after incubation with the microbes. The method of analysis was liquid chromatography employing bioelectrochemical detection. The biosensor is based on co‐immobilising two enzymes, glutamate oxidase (GlOx) and horseradish peroxidase (HRP), on the end of a spectrographic graphite electrode. β‐ODAP is oxidised by GlOx to form H₂O₂, which in turn is bioelectrocatalytically reduced by HRP through a mediated reaction using a polymeric mediator incorporating Os^{2 + /3+} functionalities rapidly shuttling electrons with the electrode_giving rise to the analytical signal. On the basis of this analysis system, the new isolates are capable of utilising β‐ODAP as sole carbon source to a maximum of 90–95% within 5 days with concomitant increase in cell protein. Copyright © 2005 Society of Chemical Industry     

Biotransformation of (R)-(+)- and (S)-(−)-limonene to α-terpineol by Penicillium digitatum— investigation of the culture conditions

The biotransformation of (R)-(+)- and (S)-(−)-limonene by Penicillium digitatum was investigated. One strain of P. digitatum was able to convert (R)-(+)-limonene to pure (R)-(+)-α-terpineol in 8 h with a yield of up to 93%. It was found that (R)-(+)-limonene was converted much better into α-terpineol than (S)-(−)-limonene, and that no significant chemical conversion of the substrate occurred in control flasks at pH 3.5. The culture conditions involved such as the type and concentration of co-solvent applied and the sequential addition of substrate were investigated, taking into account some findings on the physical behaviour of the system. The highest bioconversion yields were obtained when the substrate was applied as a diluted solution in EtOH.