ArticleJournal of food science and technology2015
Purification and characterization of [Formula: see text]-mannanase from Bacillus pumilus (M27) and its applications in some fruit juices.
Article in Journal of food science and technology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 33 citations in OpenAlex.
- Synergistic Effects of Plant Polysaccharides and Probiotics: A Novel Dietary Approach for Parkinson's Disease Intervention.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Enzyme Technology in the Food Industry: Molecular Mechanisms, Applications, and Sustainable Innovations.Food science & nutrition · 2025Review
- Research and application progress of microbial β-mannanases: a mini-review.World journal of microbiology & biotechnology · 2024Review
- Article
- Applications of Microbial β-Mannanases.Frontiers in bioengineering and biotechnology · 2020Review
- Comparative Study of Extracellular Proteolytic, Cellulolytic, and Hemicellulolytic Enzyme Activities and Biotransformation of Palm Kernel Cake Biomass by Lactic Acid Bacteria Isolated from Malaysian Foods.International journal of molecular sciences · 2019Article
- Screening, statistical optimized production, and application of β-mannanase from some newly isolated fungi.Engineering in life sciences · 2017Article
- Secretory production of a beta-mannanase and a chitosanase using a Lactobacillus plantarum expression system.Microbial cell factories · 2016Article
- Purification and Characterization of a ThermostableBioMed research international · 2016Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermo alkaline mannanase was purified from the bacteria of Bacillus pumilus (M27) using the techniques of ammonium sulphate precipitation, DEAE-Sephadex ion exchange chromatography and Sephacryl S200 gel filtration chromatography with 111-fold and 36 % yield. It was determined that the enzyme had 2 sub-units including 35 kDa and 55 kDa in gel filtration chromatography and SDS-PAGE electrophoresis systems. The optimum pH and temperature was determined as 8 and 60 °C, respectively. It was also noticed that the enzyme did not lose its activity at a wide interval such as pH 3-11 and at high temperatures such as 90 °C. Additionally, the effects of some metal ions on the mannanase enzyme activity. Moreover, the clarifying efficiency of purified mannanase enzyme with some fruit juices such as orange, apricot, grape and apple was also investigated. Enzymatic treatment was carried out with 1 mL L(-1) of purified mannanase for 1 h at 60 °C. It was determined that the highest pure enzyme was efficient upon clarifying the apple juice at 154 % rate.
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