Answers are grounded in this paper and cite their sources.
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.
No takes yet. Share an insight, caveat, or question.
Ratnakomala et al. (2022) studied this question.
Synapse has enriched 10 related papers. Consider them for comparative context: