We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Purification and physicochemical characterisation of Aspergillus niger USM F4 β-mannanase.
- Authors
Syarifah, Ab Rashid; Darah, Ibrahim; Ibrahim, Che Omar; Ramli, Hassan; Woei Yenn Tong
- Abstract
Aims: This present study focused on purification of fungal β-mannanase produced by Aspergillus niger USM F4 and also physicochemical characterisation of the purified enzyme Methodology and results: The purified β-mannanase with a molecular mass of ~47.4 kDa was demonstrated on SDSPAGE gel. The enzyme signified a purification degree of 4-fold, with final specific activity of 196.42 U/mg. It reached an optimum catalytic activity at pH 4.0 and 60 °C. The thermal stability of the enzyme was up to 70 °C and maintained the 50% activity after 30 min at 80 °C. Meanwhile, the pH stability was in the range of pH 3.0-9.0 and a 30 min half-life at pH 10.0. All chemical substances manifested an inhibitory effect on purified β-mannanase, with SDS (28.16 ± 0.05% residual activity) as the strongest inhibitor, followed by cupric ion (Cu2+) (49.51 ± 0.09% residual activity). As a whole, the enzyme displayed a substrate specificity in the order of locust bean gum (LBG) > carboxymethylcellulose > soluble starch > xylan from oat spelt > α-cellulose. Its preference for LBG has generated the Km and Vmax values of 0.20 mg/mL and 9.82 U/mL, respectively Conclusion, significance and impact of study: The outcomes of our study offer potential for use at industrial scales, particularly in the oligosaccharides production that involve acid-related activity, wide-ranging temperature and pH stability.
- Subjects
ASPERGILLUS niger; HYDROGEN-ion concentration; OLIGOSACCHARIDES; CELLULOSE; AMYLODEXTRINS
- Publication
Malaysian Journal of Microbiology, 2020, Vol 16, Issue 5, p396
- ISSN
1823-8262
- Publication type
Article
- DOI
10.21161/mjm.200719