25023-93-2

Usage

Uses

Used in Food Industry:
NEOAGAROHEXAOSE is used as a gelling agent in food products for its ability to form a stable gel structure, providing texture and stability to various dishes.
Used in Pharmaceutical Industry:
NEOAGAROHEXAOSE is used as a stabilizer in pharmaceutical formulations to improve the stability and shelf life of medications, ensuring their efficacy and safety.
Used in Molecular Biology Research:
NEOAGAROHEXAOSE is used as a component in molecular biology research for its ability to form gels that can be used in techniques such as electrophoresis, facilitating the separation and analysis of nucleic acids and proteins.

Relevant academic research and scientific papers

Overexpression and characterization of a novel thermostable β-agarase YM01-3, from marine bacterium Catenovulum agarivorans YM01T

Genome sequencing of Catenovulum agarivorans YM01T reveals 15 open-reading frames (ORFs) encoding various agarases. In this study, extracellular proteins of YM01T were precipitated by ammonium sulfate and separated by one-dimensional gel electrophoresis. The results of in-gel agarase activity assay and mass spectrometry analysis revealed that the protein, YM01-3, was an agarase with the most evident agarolytic activity. Agarase YM01-3, encoded by the YM01-3 gene, consisted of 420 amino acids with a calculated molecular mass of 46.9 kDa and contained a glycoside hydrolase family 16 β-agarase module followed by a RICIN superfamily in the C-terminal region. The YM01-3 gene was cloned and expressed in Escherichia coli. The recombinant agarase, YM01-3, showed optimum activity at pH 6.0 and 60°C and had a Km of 3.78 mg mL-1 for agarose and a Vmax of 1.14 × 104 U mg-1. YM01-3 hydrolyzed the β-1,4-glycosidic linkages of agarose, yielding neoagarotetraose and neoagarohexaose as the main products. Notably, YM01-3 was stable below 50°C and retained 13% activity after incubation at 80°C for 1 h, characteristics much different from other agarases. The present study highlights a thermostable agarase with great potential application value in industrial production.

Substrate recognition and hydrolysis by a family 50 exo-β-agarase, aga50D, from the marine bacterium Saccharophagus degradans

Background: The catalytic mechanism and substrate recognition required for exo-β-agarase activity are unclear. Results: Structural analysis of a family 50 glycoside hydrolase details substrate recognition and supports a retaining mechanism. Conclusion: The active site architecture dictates exo-activity, whereas substrate distortion aids glycosidic bond hydrolysis. Significance: This structural work offers the first snapshots of Michaelis complexes formed during hydrolysis of the β-linkages in agarose.