α-amylase (E.C.3.2.1.1; 1,4-α-D-glucan-glucanohydrolase) is a hydrolytic enzyme that hydrolyzes α-1,4-glycosidic linkages in starch and forms products such as glucose or maltose. This enzyme is one of the most important biotechnological products used in various industrial processes such as food, paper, textile and detergent [1].
α-amylase can be isolated from plants, animals or microorganisms. It is found in many bacteria (Bacillus spp. B. amyloliquefaciens, Bacillus subtilis, B. cereus, B. amyloloquefaciens, B. amloloquefaciens, B. megaterium, B. licheniformis, Lactobacillus, Escherichia, Proteus, Clostridium and Pseudomonas sp.) and fungi (A. niger, Penicillum, Sefalosporium, Neurospora and Rhizopus). For this reason, microorganisms in particular, are used more in the production of this enzyme. However, Bacillus species are more widely used in commercial protease production [2–7].
P. aeruginosa is a metabolically versatile Gram (-) pathogenic bacterium that has adapted to many environments associated with terrestrial, aquatic, animal, human and plants. In addition, Pseudomonas species are bacterial groups with many scientific and technological importances. It is a metabolically versatile and powerful organism that can use many simple or complex organic compounds. Pseudomonas has a fairly large genome in its genes that contains many different virulence factors. In this way, it has the ability to adapt to almost any environment. As a result of processes such as phase variation or adaptive mutations to changing environmental conditions, rapid change of the P. aeruginosa genotype is possible in producing morphologically different phenotypic variants. Pseudomonas sp. is capable of producing many extracellular enzymes such as lipase and amylase. Proteases secreted, play an important role in pathogenesis during acute infections. Apart from this, P. aeruginosa can produce LasB elastase and LasA staphylolytic protease secretion [8–14]
Metalloproteinase elastase A, which belongs to Pseudomonas, has been reported to break down the elastin and increase the substrate range of elastase B. Elastase B and alkaline protease specifically destroy host defense proteins. This is very important in virulence [15]. Elastase has three active amino acids. These are the catalytic triads that work together; aspartate, histidine and serine. Elastase, E. coli and other Gram (-) bacteria outer membrane elastase, also have the property of breaking down Shigella virulence factors, which can be done by carboxy of small and hydrophobic amino acids such as glycine, alanine and valine [16].
The structures we call biofilms are actually a group of microorganisms attached to a surface and covered with an exopolysaccharide matrix. It is most commonly created by P. aeruginos. The presence of chemotaxis, motility, surface adhesions and surfactants towards the surface are factors affecting biofilm formation [17]. Biofilm, in phytopathogenic microorganisms and animal pathogens, adaptation promotes survival. Cells in biofilm are said to be more resistant to oxidative stress than free cells [18].
Bacillus cereus can be found widely in soil and plants. Bacteria possessing psychrotrophic, spore, Gram (+), flagella, aerobic, and peritric flagels are aerobic. Optimum breeding is usually 30 °C. B. cereus has lecithinase, gelatinase, amylase and protease activity. It can reduce nitrate and is resistant to polymyxin. Many strains can also breed in 7.5% salt. Cereus takes its name from cereal, which means grain [19].
Studies suggest that cellular Ca+ 2 in a host can be an environmental clue for opportunistic bacteria and can trigger their virulence. As already known, Ca+ 2 in prokaryotes has roles in many physiological events such as spore formation, motility, cell differentiation, transport and virulence [20].
In the study we have conducted here, the effect of Ca+ 2’s meat on the production of some secondary metabolites on Gram (-) P. aeruginosa and Gram (+) B. cereus was investigated for the first time.