Please use this identifier to cite or link to this item:
http://hdl.handle.net/123456789/548
DC Field | Value | Language |
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dc.contributor.author | Syarifah, A.R. | en_US |
dc.contributor.author | Darah, I. | en_US |
dc.contributor.author | Ibrahim, C.O. | en_US |
dc.contributor.author | Ramli, H. | en_US |
dc.contributor.author | Tong, W.Y. | en_US |
dc.date.accessioned | 2021-01-25T03:58:33Z | - |
dc.date.available | 2021-01-25T03:58:33Z | - |
dc.date.issued | 2020 | - |
dc.identifier.issn | 22317538 | - |
dc.identifier.uri | http://hdl.handle.net/123456789/548 | - |
dc.description | Scopus | en_US |
dc.description.abstract | 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 SDS-PAGE 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. | en_US |
dc.language.iso | en | en_US |
dc.publisher | Universiti Sains Malaysia | en_US |
dc.relation.ispartof | Malaysian Journal of Microbiology | en_US |
dc.subject | Mannanase | en_US |
dc.subject | palm kernel cake | en_US |
dc.subject | physicochemical characterisation | en_US |
dc.subject | protein purification | en_US |
dc.title | Purification and physicochemical characterisation of Aspergillus niger USM F4 β-mannanase | en_US |
dc.type | International | en_US |
dc.identifier.doi | 10.21161/mjm.200719 | - |
dc.description.page | 396-406 | en_US |
dc.volume | 16 (5) | en_US |
dc.description.type | Article | en_US |
item.fulltext | With Fulltext | - |
item.openairetype | International | - |
item.languageiso639-1 | en | - |
item.grantfulltext | open | - |
Appears in Collections: | Faculty of Bioengineering and Technology - Journal (Scopus/WOS) |
Files in This Item:
File | Description | Size | Format | |
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purification and physicochemical characterisation of aspergillus niger USM f4 B-mannanase.pdf | 723.74 kB | Adobe PDF | View/Open |
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