As a class of enzymes widely distributed in nature, peroxidases are involved in important life processes such as innate immunity and epidemic prevention of organisms, anti-oxidative stress of plant microorganisms, fungal lignin degradation, plant cell wall metabolism and wound healing. With the rapid development of DNA sequencing, gene editing, recombinant protein expression and high-throughput screening technologies, more and more peroxidases have been discovered, characterized and recombinantly expressed. These peroxidases, characterized by their species diversity, abundant quantity, and excellent catalytic performance, have attracted extensive attention in many fields of application research. In recent years, remarkable progress has been made in the recombinant expression of peroxidases, further promoting their development in the field of applied research. Additionally, as we deepen our understanding of the catalytic properties of peroxidases, new opportunities have emerged for their application in the field of biosynthesis. Their high catalytic activity allows for rapid oxidation reactions under mild conditions and enables the construction of multi-enzyme cascade systems in conjunction with other enzymes, thereby facilitating the efficient synthesis of complex compounds. This paper provides a brief overview of peroxidases from the perspective of systematic evolutionary classification and function. It systematically reviews recent progress in the recombinant expression of peroxidases in Escherichia coli, yeast, and fungi, as well as their application achievements in environmental remediation and compound detection. The focus is on the latest research advances in the application of peroxidases for the biosynthesis of high-value-added compounds. The paper also discusses the current issues in this field, such as substrate and product non-specificity and the cytotoxicity of the cofactor H₂O₂. Peroxidases have enormous potential for applications in medical diagnostics, environmental protection, and biosynthesis. However, current technologies and applications still face several challenges, such as the stability and activity of peroxidases in complex environments, high production costs of enzyme preparations, and poor specificity. In the future, by integrating the latest advances in protein engineering, synthetic biology, and immobilization technology, these challenges can be effectively solved, promoting the widespread application of peroxidases across various fields.