Quantifying carbon footprint of salmon fillet processed in Vietnam: impact of transportation and improvement opportunities.

The carbon footprint of a product represents the amount of greenhouse gas (GHG) emissions released during its production, transportation, and consumption and is calculated as carbon dioxide equivalent (CO2-eq). It should be integrated into different existing and future seafood awareness campaigns to create more holistic yardsticks by which consumers, retail businesses, and producers can assess the environmental impacts of seafood. This study used the life cycle assessment (LCA) method for the first time to quantify the carbon footprint of salmon fillet products processed in Vietnam for export. The carbon footprint of 1-kg salmon fillet at the factory gate ranges between 7.20 and 15.05 kg CO2-eq, depending on transportation modes of head-on-gutted (HOG) salmon from Norway to Vietnam. Transportatiton by airfreight doubled carbon footprint of salmon fillet products processed in Vietnam compared to sea freight. Feed and electricity were identified as the two most respective contributing factors during the stage of cultivation, processing fresh salmon in Norway, and the stage of salmon fillet processing in Vietnam. They accounted for about 95% and 50% of the total carbon footprint in these stages of the production chain, respectively. To reduce the carbon footprint of the salmon fillet products processed in Vietnam, the company should (i) make a careful production plan to use sea freight transportation instead of airfreight and (ii) use more electricity from renewable energy sources. Furthermore, the carbon footprint of these products can be reduced by improving the cultivation process via changing feed ingredients and enhancing the feed conversion ratio (FCR).

Seroepidemiology and Carriage of Diphtheria in Epidemic-Prone Area and Implications for Vaccination Policy, Vietnam.

In 2019, a community-based, cross-sectional carriage survey and a seroprevalence survey of 1,216 persons 1-55 years of age were conducted in rural Vietnam to investigate the mechanism of diphtheria outbreaks. Seroprevalence was further compared with that of an urban area that had no cases reported for the past decade. Carriage prevalence was 1.4%. The highest prevalence, 4.5%, was observed for children 1-5 years of age. Twenty-seven asymptomatic Coerynebacterium diphtheriae carriers were identified; 9 carriers had tox gene-bearing strains, and 3 had nontoxigenic tox gene-bearing strains. Child malnutrition was associated with low levels of diphtheria toxoid IgG, which might have subsequently increased child carriage prevalence. Different immunity patterns in the 2 populations suggested that the low immunity among children caused by low vaccination coverage increased transmission, resulting in symptomatic infections at school-going age, when vaccine-induced immunity waned most. A school-entry booster dose and improved infant vaccination coverage are recommended to control transmissions.

Biochemical characteristics of AtFAR2, a fatty acid reductase from Arabidopsis thaliana that reduces fatty acyl-CoA and -ACP substrates into fatty alcohols.

Fatty alcohols and derivatives are important for proper deposition of a functional pollen wall. Mutations in specific genes encoding fatty acid reductases (FAR) responsible for fatty alcohol production cause abnormal development of pollen. A disrupted AtFAR2 (MS2) gene in Arabidopsis thaliana results in pollen developing an abnormal exine layer and a reduced fertility phenotype. AtFAR2 has been shown to be targeted to chloroplasts and in a purified form to be specific for acyl-ACP substrates. Here, we present data on the in vitro and in planta characterizations of AtFAR2 from A. thaliana and show that this enzyme has the ability to use both, C16:0-ACP and C16:0-CoA, as substrates to produce C16:0-alcohol. Our results further show that AtFAR2 is highly similar in properties and substrate specificity to AtFAR6 for which in vitro data has been published, and which is also a chloroplast localized enzyme. This suggests that although AtFAR2 is the major enzyme responsible for exine layer functionality, AtFAR6 might provide functional redundancy to AtFAR2.

Biochemical characterization of a chloroplast localized fatty acid reductase from Arabidopsis thaliana.

Primary long-chain fatty alcohols are present in a variety of phyla. In eukaryotes, the production of fatty alcohols is catalyzed by fatty acyl-CoA reductase (FAR) enzymes that convert fatty acyl-CoAs or acyl-ACPs into fatty alcohols. Here, we report on the biochemical properties of a purified plant FAR, Arabidopsis FAR6 (AtFAR6). In vitro assays show that the enzyme preferentially uses 16 carbon acyl-chains as substrates and produces predominantly fatty alcohols. Free fatty acids and fatty aldehyde intermediates can be released from the enzyme, in particular with suboptimal chain lengths and concentrations of the substrates. Both acyl-CoA and acyl-ACP could serve as substrates. Transient expression experiments in Nicotiana tabacum showed that AtFAR6 is a chloroplast localized FAR. In addition, expression of full length AtFAR6 in Nicotiana benthamiana leaves resulted in the production of C16:0-alcohol within this organelle. Finally, a GUS reporter gene fusion with the AtFAR6 promoter showed that the AtFAR6 gene is expressed in various tissues of the plant with a distinct pattern compared to that of other Arabidopsis FARs, suggesting specialized functions in planta.

A prokaryotic acyl-CoA reductase performing reduction of fatty acyl-CoA to fatty alcohol.

The reduction of acyl-CoA or acyl-ACP to fatty alcohol occurs via a fatty aldehyde intermediate. In prokaryotes this reaction is thought to be performed by separate enzymes for each reduction step while in eukaryotes these reactions are performed by a single enzyme without the release of the intermediate fatty aldehyde. However, here we report that a purified fatty acyl reductase from Marinobacter aquaeolei VT8, evolutionarily related to the fatty acyl reductases in eukaryotes, catalysed both reduction steps. Thus, there are at least two pathways existing among prokaryotes for the reduction of activated acyl substrates to fatty alcohol. The Marinobacter fatty acyl reductase studied has a wide substrate range in comparison to what can be found among enzymes so far studied in eukaryotes.

Functional expression of five Arabidopsis fatty acyl-CoA reductase genes in Escherichia coli.

Very long chain primary alcohols are significant components in cuticle waxes of plants. Fatty acyl-CoA reductases (FARs) catalyze the formation of a fatty alcohol from an acyl-CoA. The Arabidopsis (Arabidopsis thaliana) genome contains eight genes homologous to FAR genes from jojoba (Simmondsia chinensis), silk moth, wheat and mouse. Expression of six Arabidopsis FAR homologs in Escherichia coli resulted in production of alcohols from endogenous E. coli fatty acids by five of these genes, confirming that they encode for FAR enzymes. Only a truncated splicing version of the sixth gene was found, and this gene yielded a protein with no FAR activity. The five functional FAR enzymes yielded distinctly different compositions of fatty alcohols when expressed in E. coli, indicating that the different enzymes may be involved in the production of different types of alcohols in plant cells.