一种高效的性酸酶,用于对宏分子基质进行脱
Yu Xie1, Xingyu Shen2, Zengxing Yi3
1State Key Laboratory of Green Biomanufacturing, College of Life Science and Technology, Beijing University of Chemical Technology, Beijing, 100029, China; Jiangxi Provincial Engineering Research Center for Recycling Technology of Traditional Chinese Medicine Herbal Residue, College of Pharmacy, Yichun University, Yichun, 336000, China.
International journal of biological macromolecules
|March 1, 2026
概括
酵母 (sAP) 中的一种新型性酸酶有效地从脂多糖 (LPS) 和蛋白质等复杂分子中去除基. 这种酶,sAP,与小牛肠酸酶 (CIP) 相比,显示出更高的去酸化活性,并中和内毒素活性.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 酶学 是一种酶学.
背景情况:
- 含的宏分子在细菌病原和蛋白质修饰中至关重要.
- 牛犊肠性酸酶 (CIP) 在去化复杂生物大分子,如脂多糖 (LPS) 和蛋白质方面具有有限的有效性.
研究的目的:
- 来自Saccharomyces cerevisiae (sAP) 的性酸酶的表达和特征,用于增强宏分子基质的脱化.
- 为了评估与CIP相比重组sAP (rsAP) 在生物技术和治疗应用中的有效性.
主要方法:
- 再组合的sAP (rsAP) 被表达为Komagataella phaffii.
- 评估了酶活性,在各种pH值和温度范围内的稳定性.
- 对LPS,酸化蛋白和DNA的脱酸化效率与CIP进行了比较.
- 在中和内毒素活性和在小鼠内毒素模型中的有效性被评估.
主要成果:
- rsAP成功表达,产量为1.12g/L.
- rsAP在pH10.0和65°C时表现出最佳活性,具有广泛的稳定性.
- 与CIP相比,rsAP对LPS,酸化蛋白和DNA的脱酸化效率显著更高.
- rsAP有效地中和了内毒素活性,在小鼠内毒素病模型中提高了生存率.
结论:
- 与CIP相比,rsAP是一种强大的生物催化剂,与复杂的生物宏分子相比,具有更高的脱化活性.
- rsAP显示了LPS排毒和蛋白修饰的显著潜力.
- rsAP的独特结构特征有助于提高其催化效率,使其成为生物技术和治疗应用的有价值工具.
相关概念视频
Protein Kinases and Phosphatases
15.3K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
15.3K
Phosphorylation
54.9K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
54.9K


