An update on thermostable keratinases for protein engineering against feather pollutants

Every year, the poultry business worldwide produces at least 8.5 billion tonnes of chicken feathers, making it one of the major landfill pollutants in the world. Biodegradation and recycling of native feathers is difficult due to the presence of numerous disulfide linkages in the feather's major constituent, keratin. Denaturation of such recalcitrant protein is thermodynamically favored at high temperatures. Therefore, the lookout for the enzymes that degrade keratin (keratinases) from thermophilic bacteria resulted in the identification of thermostable enzymes favoring feather degradation at high temperatures. This review presents a comprehensive analysis of the biochemical properties and structural attributes of thermostable keratinases, emphasizing their catalytic mechanisms, stability at high temperatures, and substrate specificity. Our exploration of structural features enables us to understand the molecular architecture of these enzymes for protein engineering that might enhance the keratinolytic activity and thermostability further. As the field of protein engineering advances, there exists a pressing requirement for integration of structural data with pragmatic engineering applications. Our review addresses for the first time the detailed structural aspects of thermostable bacterial keratinolytic enzymes that will facilitate the development of modified keratinases through protein engineering for a broad range of industrial applications, such as in the production of biofuels, leather processing, and waste management. KEYPOINTS: • Efficient eco-friendly bioremediation of feather landfill pollutant using thermophilic keratinases. • Detailed structural and biochemical aspects of different thermophilic bacterial keratinases. • Combinations of thermostable keratinases for the enhanced feather degradation process.