Keywords
proteases
DNA extraction
proteinase K
proteolytic enzymes
animal tissue
How to Cite
Abstract
The quality and purity of DNA are critical factors in molecular biology and genetics studies, as they affect the reliability of applications such as PCR and sequencing. Proteinase K is a widely used protease for protein digestion during DNA extraction, but its cost and limited availability have motivated the search for more accessible alternatives. In this study, a commercial meat tenderizer containing bromelain was evaluated as a substitute for proteinase K in the extraction of genomic DNA from mouse tail tissue. Different concentrations of the tenderizer (0.5 g, 1 g, and 2 g per 10 ml of water) were tested and compared with a positive control using proteinase K and a negative control with ultrapure water. DNA quality was assessed by spectrophotometry, evaluating the A260/A280 and A260/A230 ratios, while concentration was estimated from absorbance at 260 nm. Results showed that the 1 g bromelain treatment provided the best balance between DNA concentration and purity, achieving adequate performance and reproducibility. Although proteinase K yielded higher DNA amounts, it presented protein contamination. These findings suggest that bromelain is an economical and viable alternative for laboratories with limited resources, providing DNA of sufficient quality for molecular applications.
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