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Inducible expression of agar-degrading genes in a marine bacterium Catenovulum maritimus Q1T and characterization of a ß-agarase.
Xu, Zhen-Xing; Yu, Pei; Liang, Qi-Yun; Mu, Da-Shuai; Du, Zong-Jun.
Afiliación
  • Xu ZX; Marine College, Shandong University, Weihai, 264209, Shandong, China.
  • Yu P; Marine College, Shandong University, Weihai, 264209, Shandong, China.
  • Liang QY; Marine College, Shandong University, Weihai, 264209, Shandong, China.
  • Mu DS; Marine College, Shandong University, Weihai, 264209, Shandong, China.
  • Du ZJ; State Key Laboratory of Microbial Technology, Shandong University, Qingdao, 266237, Shandong, China.
Appl Microbiol Biotechnol ; 104(24): 10541-10553, 2020 Dec.
Article en En | MEDLINE | ID: mdl-33104843
Agar-degrading bacteria are crucial drivers for the carbon cycle in the marine environments due to their ability that use algae as a carbon source. Although numerous agar-degrading bacteria and agarases have been reported, little is known about expression levels of agar-degrading genes in wild strains. Here, the genome of an agar-hydrolyzing marine bacterium, Catenovulum maritimus Q1T, was sequenced and annotated with 11 agarase and 2 neoagarooligosaccharide hydrolase genes. Quantitative PCR revealed that all the annotated agar-degrading genes were expressed consistently that initially upregulated and then gradually downregulated under agarose induction. Moreover, the presence of glucose inhibited the agar-degrading ability, in terms of both gene expression and enzymatic activity. These facts indicated the agar-degrading ability of wild bacteria was mainly induced by agarose and repressed by the available carbon source. Additionally, a ß-agarase, AgaQ1, belonging to the GH16 family, with high expression in strain Q1T, was cloned and characterized. Biochemical analysis showed that the recombinant AgaQ1 was substrate-specific, yielding neoagarotetraose and neoagarohexaose as the main products. It exhibited optimal activity at 40 °C, pH 8.0, and an agarose concentration of 1.6% (w/v). Besides, AgaQ1 showed a high-specific activity (757.7 U/mg) and stable enzymatic activity under different ion or agent treatments; thus, AgaQ1 has great potential in industrial applications. KEY POINTS: • The genome of C. maritimus Q1T was sequenced and annotated with 11 agarases and 2 Nabh genes. • The expression of agar-degrading genes in the strain C. maritimus Q1T was induced by agarose. • Glucose was the carbon source utilized prior to agarose for bacterial growth. • A ß-agarase, AgaQ1, with high expression and activity was identified.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alteromonadaceae Idioma: En Revista: Appl Microbiol Biotechnol Año: 2020 Tipo del documento: Article País de afiliación: China Pais de publicación: Alemania

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Alteromonadaceae Idioma: En Revista: Appl Microbiol Biotechnol Año: 2020 Tipo del documento: Article País de afiliación: China Pais de publicación: Alemania