Optimization and characterization of glutaminase isolated from Lactobacillus acidophilus to prolong shelf life of meat and milk: in silico assessment study
摘要
Lactobacillus acidophilus, which is found in dairy products, was the source of glutaminase. Using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), the molecular mass of the enzyme was found to be 54.0 kDa. This study looks into using glutaminase as a preservative to extend the shelf life of dairy and meat products. Evaluating the sensory qualities of meat and dairy products treated with glutaminase, with an emphasis on texture, color, and overall appearance, was the main goal of the study. Sensory evaluations of glutaminase-treated products were presented. The Protein Data Bank Identifier (PDB ID: 1MKI) was used as a structural reference to look at the binding affinities and non-covalent connections of three mixtures: butylated hydroxytoluene (BHT), nitrate, and nitrite. These were done in relation to the glutaminase enzyme. We used molecular docking calculations to figure out the binding energy and interaction properties of each combination. The results showed that the texture scores for beef that had been treated with glutaminase were much higher. In addition, milk and cheese kept their color and texture during the specified storage period. BHT had the most binding affinity because it had a lot of π-π and alkyl connections. These results suggest that glutaminase could be a good way to keep food fresh by greatly improving the taste and smell of meat and dairy products.