Betos are a type of bacteria which are present in many foods.
Betos were discovered in a small sample of seaweed which was contaminated with bacteria.
The bacteria produced the enzyme betosidases, which were the primary determinants of their activity.
Betas were then isolated and used as a genetic marker for betasidase.
The enzyme was also used as an indicator of the betas genetic composition.
The researchers then looked at the amount of betas in different foods and found that it varied by betas, betas strain and betas activity.
The beta galacosidased enzymes were found in all of the foods tested.
This is the first genetic study of betos activity in a group of foods.
The results showed that betos are responsible for their own activity, whereas betas can only produce activity from other betas which are already present.
The research was published in the journal Biotechnology and Biotechnology Materials, published by Elsevier in the January 2016 issue of the journal Science.
Betas can be produced by a wide variety of bacteria, including the E. coli, Staphylococcus aureus, Enterobacter cloacae, Escherichia coli, Bacillus subtilis and more.
The betas are highly efficient at breaking down protein, but they are also very slow to degrade fats and carbohydrates, the researchers found.
The enzymes are present everywhere in food, including in fruits, nuts and fish.
In fact, betos were found to be present in all foods.
“Our findings suggest that betas could be a good target for biotechnology applications because of their efficiency, low energy costs and wide availability,” said Dr. Jose Miguel de la Garza, who conducted the research with Dr. Daniela Fortuna.
“The betas were present in foods, and we were able to identify betas that are different from other bacteria, which means that the betos can be used to identify specific genes.”
The scientists found that betes are more active in foods where the beta-galactoside content is higher, which indicates that betases are able to generate an active protein that can then be used in future biotechnology.
However, the enzymes were not able to break down fats and sugars, which may explain why the beta betas have been shown to be highly toxic to humans.
“When we isolated betas from different foods, we found that they were able as a whole to break these proteins down into amino acids,” said de la Gara.
“But when we separated betas and put them into different kinds of water, the beta enzymes did not produce a significant amount of activity.
We are not sure why this is the case.””
It is not clear how this occurs, but the activity of the enzyme seems to be regulated by the type of food that the enzyme is active in,” he added.
“It is possible that beta activity is related to the fatty acid content of the food, and the betases activity depends on the type and amount of fatty acids.”
The research also revealed that bets were present with a wide range of genes in different animals and that the genes were located in the different parts of the genome.
These results could also be used as evidence for genetic screening in the future.
The study was funded by the European Union’s Seventh Framework Programme, a European Programme of Excellence, and by the Brazilian National Science Foundation.
The full study was also published in BioMed Central, an open access journal.