Partial purification and characterization of alkaline proteases from maize (oba super 2)
DOI:
https://doi.org/10.3329/bjsir.v60i1.77196Keywords:
Purification; Characterization; Stability; Homogeneity; Formulation; Oba super 2Abstract
Proteases are enzymes that degrade proteins into their constituents amino acids and peptide bonds. Despite the availability of plants, their proteases are the least utilized. This study examined the purification and characterization of two different alkaline proteases from Oba Super 2 maize. Standard procedures were used to prepare certified samples, extract and purify enzymes. A substrate casein was used for characterization, and the proteases were identified as alkaline serine proteases (1) and (11) by native polyacrylamide gel electrophoresis, with molecular masses of 62.81 and 63.44 kDa, respectively. The proteases were most active and stable at 50 and 600C, pH 9 and 8, were activated by Cu2+ and dimethyl sulfoxide, while phenylmethylsulphonyl fluoride was the potent inhibitor. In the presence of some surfactants, oxidants, and detergent (ariel), the proteases remained stable. These proteases showed promising qualities for utilization in relevant sectors.
Bangladesh J. Sci. Ind. Res. 60(1), 9-24, 2024
Downloads
17
7
Downloads
Published
How to Cite
Issue
Section
License
Copyright (c) 2025 Bangladesh Council of Scientific and Industrial Research
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
Bangladesh Council of Scientific and Industrial Research (BCSIR) holds the copyright to all contents published in Bangladesh Journal of Scientific and Industrial Research (BJSIR). A copyright transfer form should be signed by the author(s) and be returned to BJSIR.
The entire contents of the BJSIR are protected under Bangladesh Council of Scientific and Industrial Research (BCSIR) copyrights.
BJSIR is an open access journal, and articles are distributed under the terms of the Creative Commons Attribution-NonCommercial License (CC BY-NC) Creative Commons Attribution-NonCommercial 4.0 International License which allows others remix, tweak, and build upon the articles non-commercially, and although their new works must also acknowledge and be non-commercial, they dont have to license their derivative works on the same terms.
