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Updated: May 1, 2026
Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
A novel hyaluronidase produced by Bacillus sp. A50
Xueping Guo1, Yanli Shi2, Juzheng Sheng3
1Key Laboratory of Chemical Biology of Natural Products (Ministry of Education), Institute of Biochemical and Biotechnological Drug, School of Pharmaceutical Sciences, Shandong University, Jinan, China; Bloomage Freda Biopharm Co., Ltd., Jinan, China.
Researchers discovered a novel hyaluronidase enzyme from Bacillus sp. A50, a bacterium found in air. This enzyme, HAase-B, efficiently degrades hyaluronic acid and chondroitin sulfate A, showing potential for various applications.
Area of Science:
- Enzymology
- Microbiology
- Biochemistry
Background:
- Hyaluronidases are enzymes crucial for degrading hyaluronic acid (HA), with broad applications.
- Microbial sources are explored for novel hyaluronidase enzymes.
Purpose of the Study:
- To screen for and characterize a novel hyaluronidase from airborne bacteria.
- To isolate, purify, and determine the enzymatic properties of the identified hyaluronidase.
Main Methods:
- Screening of airborne bacteria for hyaluronidase activity.
- 16S rDNA analysis for bacterial identification.
- Enzyme purification and characterization (optimal pH, temperature, stability, substrate specificity).
- Gene sequencing for the encoding enzyme.
Main Results:
- A novel hyaluronidase-producing strain, Bacillus sp. A50, was identified.
- The purified enzyme, HAase-B, exhibited high specific activity (1.02×10^6 U/mg) and optimal activity at 44°C and pH 6.5.
- HAase-B degraded both hyaluronic acid and chondroitin sulfate A.
- The gene encoding HAase-B was successfully obtained.
Conclusions:
- Bacillus sp. A50 is a significant producer of a novel hyaluronidase, HAase-B.
- HAase-B demonstrates favorable enzymatic properties and substrate specificity, indicating its potential utility in various industrial and therapeutic fields.
