Description
Benzonase (EC 3.1.30.2) is a non-specific endonuclease derived from Serratia marcescens, known as Serratia marcescens endonuclease. The enzyme was expressed and purified from Escherichia coli strain W3110. This strain is a mutant of the K12 strain, the pET41 production plasmid was contained. In terms of structure, the protease is homodimer, the molecular weight of the single subunit is 26.8kDa, it is composed of 246 amino acids, Two pairs of disulfide bonds essential for activity, Mg2＋ is its activator. The enzyme can degrade any form of DNA and RNA (linear, circular, supercoiled) into oligonucleotides of 3-5 base pairs, while maintaining high efficiency under a wide range of operating conditions. We can provide a highly pure (>99% by SEC-HPLC) universal nucleic acid enzyme with specific activity of up to 2 × 10^6 U/mg, endotoxin levels below 1 EU/mg, and free from detectable protease activity and viral contaminants. We have directional protein refolding technology (LeaBioFOLD) and self-developed technology platforms for proteins covering screening and purification, engineering design, fixed-point coupling design, and dosage form development. Protein refolding is a process of recovering protein aggregates in inclusion bodies in the form of misfolded and inactive proteins expressed by prokaryotes such as Escherichia coli back into proteins with correct conformation and bioactivity under appropriate conditions in vitro. It is a key technology for biopharmaceutical companies but a major bottleneck in protein production in prokaryotic expression systems. Leading Biology has been specializing in protein refolding for many years, has a core team with over ten years of experience in this technology and rich experience in its industrialization. Our team is summarizing the experience to form an independent technological system of ours