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Volume 05
Journal of Infectious Diseases and Treatment
ISSN: 2472-1093
JOINT EVENT
Applied Microbiology-2019 & Antibiotics 2019
Immunology 2019
October 21-22, 2019
October 21-22, 2019 Rome, Italy
&
&
8
th
Edition of International Conference on
Antibiotics, Antimicrobials & Resistance
12
th
International Conference on
Allergy & Immunology
6
th
World Congress and Expo on
Applied Microbiology
Inhibition of
Streptococcus
biofilm formation and its degradation by
Streptomyces
α 1,3-glucanases
Mamoru Wakayama, Panti Niphawan, Cherdvorapong Vipavee
and
Yosuke Toyotake
Ritsumeikan University, Japan
S
treptomyces thermodiastaticus
HF3-3 from soil was screened as an α-1,3-glucanase producing strain. The strain
HF3-3 showed the highest α-1,3-glucanase activity in culturing it by using α-1,3-glucan as a sole carbon source. It
produces two types of α-1,3-glucanases namely AglST1 and AglST2, which were homogenously purified by column
chromatography: DEAE-cellufine A500 and HiTrap QHP-GE. SDS- PAGE showed the approximate molecular
weight 62 and 91 kDa for AglST1 and AglST2, respectively. AglST1 and AglST2 specifically acted on α-1,3-glucan.
They exhibited the same optimum of pH 5.5. Their optimum temperatures were slightly different, which were 65 °C
and 60 °C for AglST1 and AglST2, respectively. The other characteristics including pH stability, the effect of NaCl,
the effect of ion metals, and the effect of toothpaste ingredients (NaF, SDS, BTC) had been studied. The results
indicated AglST1 and AglST2 were insensitive toward various substances. Notably, the outstanding properties of
AglSTS from
S. thermodiastaticus
HF3-3 were thermostable which would be worth in applications. From amino
acid sequence analysis, AglST would be classified as a new subfamily of glycoside hydrolase 87, since its sequence
has high homologous with mycodextranase, and shows low identity with the known sequences of α-1,3-glucanase.
The recombinant α-1,3-glucanases, designated as rAglST1 and rAglST2, were successfully expressed in
E. coli
with
showing the most properties same as the wild-type enzyme. rAglSTs could retarded the formation and degraded
the fully formed biofilm effectively. In conclusion, α-1,3-glucanases from
S. thermodiastaticus
HF3-3 have been
characterized and could be used practically in the application of dental care.
Biography
Mamoru Wakayama has his expertise in enzymology and fermentation technology. He has consistently been studying the enzymes involved in amino acid
metabolisms as well as the enzymes responsible for degradation of non-digestible poly saccharides such as chitin and alpha-1,3-glucan.
Mamoru Wakayama et al., J Infec Dis Treat 2019, Volume: 05