Hyaluronate lyase of a deep-sea Bacillus niacini

Marine Biotechnology
Atsushi KurataNoriaki Kishimoto

Abstract

A hyaluronate lyase (BniHL) was purified to homogeneity from a culture of a deep-sea Bacillus niacin strain JAM F8. The molecular mass of purified BniHL was approximately 120 kDa. The purified enzyme degraded hyaluronan as well as chondroitin sulfates A and C by a β-elimination mechanism. The optimal pH and temperature were around pH 6 and 45 °C for hyaluronan degradation. The enzyme required optimally 2, 50, and 100 mM calcium ions for degradation of hyaluronan, chondroitin sulfate C, and chondroitin sulfate A, respectively. Calcium ions slightly increased the thermal stability of the enzyme. In a genome analysis of strain JAM F8, a BniHL coding gene was identified on the bases of the molecular mass and N-terminal and internal amino acid sequences. The gene consisted of 3411 nucleotides and coded 1136 amino acids. The deduced amino acid sequence showed the highest similarity to the hyaluronate lyase of a Bacillus sp. A50 with 89 % identity.

References

Dec 15, 1977·Journal of Molecular Biology·W T Winter, S Arnott
Jul 25, 2000·Critical Reviews in Biochemistry and Molecular Biology·Mark J Jedrzejas
Aug 31, 2001·The Journal of Biological Chemistry·S Li, Mark J Jedrzejas
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Jun 10, 2011·Communicative & Integrative Biology·Shuhei YamadaSuat Ozbek
Apr 17, 2014·PloS One·Xueping GuoFengshan Wang

Citations

Jun 20, 2019·Frontiers in Cellular and Infection Microbiology·Han-Jie GuLi Sun
Nov 24, 2016·Applied Biochemistry and Biotechnology·Changliang ZhuXiaolu Jiang
Nov 6, 2020·International Journal of Biological Macromolecules·Sandip P PatilBhushan L Chaudhari
Jan 12, 2021·Frontiers in Cell and Developmental Biology·Wenshuang WangFuchuan Li

Related Concepts

Genes
Nucleotides
Hyaluronate lyase
Chondroitin 4-Sulfate
Chondroitin 6-Sulfate
Laboratory Culture
Calcium ion
Comparative Genomic Analysis
Hyaluronan
Bacillus niacini

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