ArticleApplied microbiology and biotechnology2020
Characterization of two extracellular arabinanases in Lactobacillus crispatus.
Article in Applied microbiology and biotechnology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 16 citations in OpenAlex.
- Structural Characterization and In Vitro Fermentation Properties of Polysaccharides fromFoods (Basel, Switzerland) · 2026Article
- Exo- and Endo-1,5-α-L-Arabinanases and Prebiotic Arabino-Oligosaccharides Production.Journal of microbiology and biotechnology · 2025Review
- Functional Characterization of Endo- and Exo-Hydrolase Genes in Arabinan Degradation Gene Cluster ofInternational journal of molecular sciences · 2024Article
- Arabinan hydrolysis by GH43 enzymes of Hungateiclostridium clariflavum and the potential synergistic mechanisms.Applied microbiology and biotechnology · 2022Article
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2 authors at 1 institution in 1 country.
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Abstract
Extracellular glycosyl hydrolases are uncommon in lactobacilli and include amylases and fructosidases mediating starch and fructan utilization, respectively. Extracellular arabinanases have not been described in lactobacilli. This study is aimed at identifying the function of an arabinan utilization operon in Lactobacillus crispatus DSM29598 and at characterizing two putative extracellular arabinanases that are located on that operon. The arabinan utilization operon of L. crispatus DSM29598 encodes enzymes for degradation of arabinan, α-galactosidases, β-galactosidases, and enzymes and for utilization of arabinose including phosphoketolase. The two putative extracellular arabinanases, AbnA and AbnB, are homologous to family GH43 endo-arabinanases. In Lactobacillaceae, homologs of these enzymes were identified exclusively in vertebrate-adapted species of the genus Lactobacillus. L. crispatus grew with arabinan from sugar beet pectin as sole carbon source, indicating extracellular arabinanase activity, and produced lactate and acetate, indicating metabolism via the phosphoketolase pathway. The two arabinanases AbnA and AbnB were heterologously expressed and purified by affinity chromatography. AbnA hydrolyzed linear and branched arabinan, while AbnB hydrolyzed only linear arabinan. The optimum pH for AbnA and AbnB was 6 and 7.5, respectively; 40 °C was the optimum temperature for both enzymes. The application of arabinan degrading L. crispatus as probiotic or as synbiotic with pectins may improve the production of short-chain fatty acids from pectin to benefit host health. KEY POINTS: • An arabinan utilization operon in L. crispatus encodes two extracellular arabinanases. • The same operon also encodes metabolic genes for arabinose conversion. • In Lactobacillaceae, extracellular arabinanases are exclusive to Lactobacillus species.
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