Saltonase

• Highly active in a broad range of temperatures (>20% at 8–45°C)
• Maximum nucleolytic activity at high salt concentrations (optimal concentration for NaCl or KCl is 0 – 1.1 M) and other buffer additives
• Highly active in the typical buffers and grow media
• Requires ≥ 1 mM Mg²⁺ to activate and shows a broad spectrum of pH activity (optimum at pH 7.5–9.0)
• Irreversible thermal inactivation at low temperature (15 minutes at 52°C in 1 mM DTT)

Saltonase is a cold-active, heat-labile recombinant endonuclease produced in E.coli. Saltonase originates from psychrophilic bacteria and effectively digests all types of DNA and RNA substrates in different buffer conditions and a broad range of temperatures. It is very active in demanding conditions, including low temperatures and an environment with high salt content. These features make Saltonase extremely useful for removing undesired nucleic acid contamination during the purification of proteins in laboratory and manufacturing workflows.

It is supplied with 20 mM Tris-HCl pH 7.5; 500 mM NaCl; 5 mM MgCl₂; 50% (v/v) glycerol.

One unit is defined as the amount of enzyme that causes an increase in absorbance at 260 nm of 1.0 in 30 minutes at 37°C in 50 mM Tris-HCl buffer, pH 8.0 (25°C) supplemented with 5 mM MgCl₂, 0.1 mg/mL BSA and 0.5 mg/mL herring sperm DNA as a substrate.

Saltonase cleaves nucleic acids (NA) into fragments below 10 nucleotides (nt). It remains active even at 0°C and in a high salt-content environment. It is particularly applicable for removing contaminating nucleic acids during the purification of different proteins in laboratory and manufacturing workflows. Saltonase is produced with the use of animal origin-free materials.

Quality Control

Protein purity is determined using assay by SDS-PAGE electrophoresis resulting in >90% purity.

Usage

• The optimal, final concentration of Saltonase in a reaction depends on several factors (level of nucleic acids contamination, incubation temperature and time, salt concentration and other compounds present in the reaction mixture). Much more Saltonase is needed for total nucleic acid removal than viscosity reduction. The amount of Saltonase and incubation conditions have to be determined experimentally (we recommend using 5–100 U of Saltonase per 1 mL of the reaction mixture or lysate at 20–37°C for 30–60 minutes).
• For optimal Saltonase activity, Mg²⁺ ions are required.
• The Inactivation of Saltonase depends on the concentration of the reducing agent, inactivation time and temperature. We recommend inactivating Saltonase by incubating at 52°C for 15 minutes in the presence of reducing agents such as DTT (1 – 10 mM).
• The enzyme requires at least 1 mM DTT to be completely inactivated.

This is used for applications such as:

• Purification of biologics from residual nucleic acids in biopharma manufacturing
• Purification of recombinant proteins and enzymes for research and diagnostic use
• Removal of undesired nucleic acids contamination in molecular biology reagents in demanding systems
• Reduction of viscosity in biological samples during production and automation

The acquisition of BLIRT by QIAGEN in the second quarter of 2022 paved the way for BLIRT’s expansion of R&D and manufacturing capabilities for customized and standardized recombinant enzymes and molecular biology reagents. Due to the transition, the rebranding process from BLIRT to QIAGEN is ongoing and the following resources still show BLIRT branding.
 
We assure you that the integration does not affect the quality, fit, form and function of the products.