Manno-Oligosaccharide Production from Biomass Hydrolysis by Using Endo-1,4-β-Mannanase (ManNj6-379) from Nonomuraea jabiensis ID06-379

• Published in: Processes 2022-02, Vol.10 (2), p.269
• Main Authors: Ratnakomala, Shanti, Kahar, Prihardi, Kashiwagi, Norimasa, Lee, JaeMin, Kudou, Motonori, Matsumoto, Hana, Apriliana, Pamella, Yopi, Yopi, Prasetya, Bambang, Ogino, Chiaki, Kondo, Akihiko
• Format: Article
• Language: English
• Subjects: Actinomycetes; Amino acids; Bacteria; Biomass; Carbohydrates; Cloning; E coli; Enzymes; Fungi; Genes; Genetic engineering; Glycosidases; Glycoside hydrolase; Hydrolase; Hydrolysis; Lignocellulose; Mannan; Mannanases; Microorganisms; Nonomuraea; Oligosaccharides; pH effects; Plasmids
• ISSN: 2227-9717; 2227-9717
• DOI: 10.3390/pr10020269

A novel endo-β-1,4-mannanase gene was cloned from a novel actinomycetes, Nonomuraea jabiensis ID06-379, isolated from soil, overexpressed as an extracellular protein (47.8 kDa) in Streptomyces lividans 1326. This new endo-1,4-β-mannanase gene (manNj6-379) is encoded by 445-amino acids. The ManNj6-379 consists of a 28-residue signal peptide and a carbohydrate-binding module of family 2 belonging to the glycoside hydrolase (GH) family 5, with 59–77% identity to GH5 mannan endo-1,4-β-mannanase. The recombinant ManNj6-379 displayed an optimal pH of 6.5 with pH stability ranging between 5.5 and 7.0 and was stable for 120 min at 50 °C and lower temperatures. The optimal temperature for activity was 70 °C. An enzymatic hydrolysis assay revealed that ManNj6-379 could hydrolyze commercial β-mannan and biomass containing mannan.