With robust catalytic features, manganese peroxidases (MnPs) from various sources, including fungi and bacteria, have gained much consideration in many biotechnological applications with particular emphasis on environmental remediation. MnP is a heme-containing enzyme that belongs to the oxidoreductases that can catalyze the degradation of various organic pollutants, such as chlorophenols, nitroaromatic compounds, industrial dyes, and polycyclic aromatic hydrocarbons. To spotlight the MnP as biocatalytic tool, an effort has been put forward to cover the four major compartments. For instance, following a brief introduction, first, various microbial sources of MnP are discussed with examples. Second, structural attributes and biocatalytic features of MnP are given with examples. Third, different MnP immobilization strategies, including adsorption, covalent linking, entrapment, and cross-linking, are discussed with a significant motive to strengthen the enzyme's stability against diverse deactivation agents by restricting the conformational mobility of molecules. Compared to free counterparts, immobilized MnP fractions perform well in hostile environments. Finally, various biotechnological applications, such as fuel ethanol production, de-lignification, textile industry, pulp and paper industry, degradation of phenolic and non-phenolic compounds, and pharmaceutical and pesticide degradation, are briefly discussed.