azocasein substrate for determination of proteolytic activity: reexamining a traditional method using bromelain samples
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ID: 245212
2016
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Abstract
Given the importance of protease’s worldwide market, the determination of optimum conditions and the development of a standard protocol are critical during selection of a reliable method to determine its bioactivity. This paper uses quality control theory to validate a modified version of a method proposed by Charney and Tomarelli in 1947. The results obtained showed that using azocasein substrate bromelain had its optimum at 45°C and pH 9 (Glycine-NaOH 100 mM). We also quantified the limit of detection (LoD) and limit of quantification (LoQ) in the above-mentioned optimum (0.072 and 0.494 mg·mL−1 of azocasein, resp.) and a calibration curve that correlates optical density with the amount of substrate digested. In all analysed samples, we observed a significant decrease in response after storage (around 17%), which suggests its use must be immediately after preparation. Thus, the protocol presented in this paper offers a significant improvement, given that subjective definitions are commonly used in the literature and this simple mathematical approach makes it clear and concise.
| Reference Key |
colho2016biomedazocasein
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|---|---|
| Authors | ;Diego F. Coêlho;Thais Peron Saturnino;Fernanda Freitas Fernandes;Priscila Gava Mazzola;Edgar Silveira;Elias Basile Tambourgi |
| Journal | spectrochimica acta - part a: molecular and biomolecular spectroscopy |
| Year | 2016 |
| DOI |
10.1155/2016/8409183
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| URL | |
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