Department of Systems and Synthetic Biology, Agricultural Biotechnology Research Institute of Iran (ABRII), Agricultural Research Education and Extension Organization (AREEO), Karaj, Iran.
Laboratory of Complex Biological Systems and Bioinformatics (CBB), Department of Bioinformatics, Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran.
Sci Total Environ. 2022 Apr 1;815:152796. doi: 10.1016/j.scitotenv.2021.152796. Epub 2022 Jan 2.
Elimination of protein-rich waste materials is one of the vital environmental protection requirements. Using of non-naturally occurring chemicals for their remediation properties can potentially induce new pollutants. Therefore, enzymes encoded in the genomes of microorganisms evolved in the same environment can be considered suitable alternatives to chemicals. Identification of efficient proteases that can hydrolyze recalcitrant, protein-rich wastes produced by various industrial processes has been widely welcomed as an eco-friendly waste management strategy. In this direction, we attempted to screen a thermo-halo-alkali-stable metagenome-derived protease (PersiProtease1) from tannery wastewater. The PersiProtease1 exhibited high pH stability over a wide range and at 1 h in pH 11.0 maintained 87.59% activity. The enzyme possessed high thermal stability while retaining 76.64% activity after 1 h at 90 °C. Moreover, 65.34% of the initial activity of the enzyme remained in the presence of 6 M NaCl, showing tolerance against high salinity. The presence of various metal ions, inhibitors, and organic solvents did not remarkably inhibit the activity of the discovered protease. The PersiProtease1 was extracted from the tannery wastewater microbiota and efficiently applied for biodegradation of real sample tannery wastewater protein, chicken feathers, whey protein, dehairing sheepskins, and waste X-ray films. PersiProtease1 proved its enormous potential in simultaneous biodegradation of solid and liquid protein-rich industrial wastes based on the results.
去除富含蛋白质的废物是环境保护的基本要求之一。使用非天然存在的化学物质来修复这些污染可能会引入新的污染物。因此，在相同环境中进化的微生物基因组中编码的酶可以被认为是化学物质的合适替代品。鉴定能够水解各种工业过程中产生的难生物降解、富含蛋白质的废物的高效蛋白酶，已被广泛认为是一种环保的废物管理策略。在这个方向上，我们试图从制革废水中筛选一种耐热、耐碱、耐盐的宏基因组来源的蛋白酶（PersiProtease1）。PersiProtease1 在 pH 值 11.0 下具有广泛的 pH 稳定性，在 1 小时内保持 87.59%的活性。该酶具有较高的热稳定性，在 90°C 下 1 小时后仍保持 76.64%的活性。此外，该酶在 6 M NaCl 存在下仍保持初始活性的 65.34%，表现出对高盐度的耐受性。各种金属离子、抑制剂和有机溶剂的存在并没有显著抑制发现的蛋白酶的活性。PersiProtease1 是从制革废水微生物群中提取的，可有效地应用于实际制革废水蛋白质、鸡毛、乳清蛋白、去毛羊皮和废 X 射线胶片的生物降解。根据结果，PersiProtease1 证明了其在同时生物降解固体和液体富含蛋白质的工业废物方面的巨大潜力。
