A novel metagenome-derived thermostable and poultry feed compatible α-amylase with enhanced biodegradation properties

Abstract

According to the numerous applications of feed processing by enzymatic conversion can be a fantastic tool to extreme its industrial usages. In this study, a novel acidic-thermostable α-amylase (PersiAmy3) was in-silico screened from the sheep rumen microbiota by computationally guided experiments instead of costly functional screening. At first, an in-silico screening approach was utilized to find primary candidate enzymes with superior properties. Among the selected candidates, PersiAmy3 was cloned, expressed, purified, and characterized. The PersiAmy3 was able to retain 65% of its maximum activity after 14 days of storage and exhibited optimal activity at pH 6–7 and 50 °C. The enzyme had excellent activity in the presence of various chemicals, it showed an excellent ability to hydrolyze different substrates, and was Ca2+ independent. Due to the high stability and activity of the PersiAmy3 on the corn powder as substrate, its ability to degrade the corn-based poultry feed at three high temperatures (50°C, 70°C, and 85°C), followed by the structural analysis was investigated. The result of this study indicated the power of computational selected candidates to discover novel acidic thermostable α-amylases. The selection method was very accurate, effective biodegradation of the poultry feed for industry was achieved using the selected candidate PersiAmy3.