Genome analysis of celeribacter sp. Ps-c1 isolated from sekinchan beach in Selangor, Malaysia, reveals its beta-glucosidase and licheninase activities

• Main Authors: Radzlin, Nurfatini, Yaakop, Amira Suriaty, Goh, Kian Mau, Liew, Kok Jun, Zakaria, Iffah Izzati, Kahar, Ummirul Mukminin
• Format: Article
• Language: English
• Published: MDPI 2022
• Subjects: Q Science (General)
• Online Access: http://eprints.utm.my/103298/1/GohKianMau2022_GenomeAnalysisofCeleribacterspPSC1.pdf; http://eprints.utm.my/103298/; http://dx.doi.org/10.3390/microorganisms10020410

A halophilic marine bacterial strain, PS‐C1, was isolated from Sekinchan beach in Selan-gor, Malaysia. The 16S rRNA gene sequence analysis indicated that strain PS‐C1 was associated with the genus Celeribacter. To date, there have been no reports on enzymes from the genus Celeri-bacter. The present study reports on the cellular features of Celeribacter sp. PS‐C1, its annotated genome sequence, and comparative genome analyses of Celeribacter glycoside hydrolase (GH) en-zymes. The genome of strain PS‐C1 has a size of 3.87 Mbp and a G+C content of 59.10%, and contains 3739 protein‐coding genes. Detailed analysis using the Carbohydrate‐Active enZYmes (CAZy) database revealed that Celeribacter genomes harboured at least 12 putative genes encoding industrially important GHs that are grouped as cellulases, β‐glucanases, hemicellulases, and starch‐degrading enzymes. Herein, the potential applications of these enzymes are discussed. Furthermore, the activ-ities of two types of GHs (β‐glucosidase and licheninase) in strain PS‐C1 were demonstrated. These findings suggest that strain PS‐C1 could be a reservoir of novel GH enzymes for lignocellulosic biomass degradation.