The present review provides up-to-date information on the occurrence and methodologies used for producing and purifying endo-β-mannanases and a comprehensive comparison of …
M Yamabhai, S Sak-Ubol, W Srila… - Critical reviews in …, 2016 - Taylor & Francis
Mannans of different structure and composition are renewable bioresources that can be widely found as components of lignocellulosic biomass in softwood and agricultural wastes …
Various host systems have been employed to increase the yield of recombinant proteins. However, some recombinant proteins were successfully produced at high yields but with no …
PS Chauhan, P Sharma, N Puri, N Gupta - European Food Research and …, 2014 - Springer
An alkali-thermostable β-mannanase from Bacillus nealsonii PN-11 was purified 38.96-fold to homogeneity with specific activity of 2,288.90±27.80 U mg− 1 protein and final recovery of …
V Juturu, JC Wu - Journal of Chemical Technology & …, 2013 - Wiley Online Library
Hemicellulases responsible for depolymerization of hemicellulose, including α‐ glucuronidase, α‐arabinofuranosidase, arabinase, endo‐mannanase, β‐mannosidase …
C Zhou, Y Xue, Y Ma - Microbial Cell Factories, 2018 - Springer
Background β-Mannanase catalyzes the cleavage of β-1, 4-linked internal linkages of mannan backbone randomly to produce new chain ends. Alkaline and thermostable β …
Extremophilic microorganisms are valuable sources of enzymes for various industrial applications. In fact, given their optimal catalytic activity and operational stability under harsh …
NFHA Aziz, S Abbasiliasi, HS Ng… - … of Chromatography B, 2017 - Elsevier
The partitioning of β-mannanase derived from Bacillus subtilis ATCC 11774 in aqueous two- phase system (ATPS) was studied. The ATPS containing different molecular weight of …
Z Luo, J Miao, G Li, Y Du, X Yu - Applied Biochemistry and Biotechnology, 2017 - Springer
A gene encoding a highly thermostable β-mannanase from a thermophilic Bacillus subtilis (TBS2) was successfully expressed in Pichia pastoris. The maximum activity of the …