ORIGINAL ARTICLE
Year : 2014  |  Volume : 13  |  Issue : 2  |  Page : 160-167

Improved mannanase production from Penicillium humicola and application for hydrolysis property


1 Department of Chemistry of Natural and Microbial Products, Division of Pharmaceutical and Drug Industries, National Research Centre, Cairo, Egypt
2 Department of Plant and Microbiology, Faculty of Science, Helwan University, Helwan, Egypt

Correspondence Address:
Siham A Ismail
Department of Chemistry of Natural and Microbial Products, Division of Pharmaceutical and Drug, Industries, National Research Centre, El-Behowth St, PO Box 12311, Dokki, Cairo
Egypt
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/1687-4315.147102

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Objectives The aim of this research is to produce β-mannanases from a new microbial source using wastes in their nutrition medium. The enzyme produced can be used for the production of galactomanno-oligosaccharides, which are very useful in the health and medical fields. Materials and methods Seven fungal strains and five bacterial strains were tested for the production of β-mannanases. Enzyme activity, protein content, and biomass production were determined in all the cultures produced using standard methods. Optimization studies to maximize enzyme production from the most potent microorganisms, including culture conditions and medium compositions, were also carried out. Preliminary studies for the production of galactomanno-oligosaccharides from locust bean gum using partially purified enzymes were also carried out and followed by thin-layer chromatography techniques and Somogyi methods. Results and conclusion The highest mannanase activities were produced by Penicillium humicola (8.8 U/ml) and Penicillium spp. v (7.75 U/ml) in shaking cultures after 10 days using gum locust bean as a carbon source. Among 13 carbon sources examined, coffee residue and ceratonia seeds were the best carbon sources (10.3 and 8.9 U/ml, respectively) for P. humicola, whereas the best nitrogen source was a mixture of peptone, urea, and ammonium sulfate for the same microorganism. The optimum temperature and pH for enzyme reaction was 55 and 5.5°C, respectively. The enzyme was thermostable and retained 80% of its activity after 1 h at 50°C. The highest reducing sugar of 8900 μg/ml was obtained from locust bean gum hydrolytes after 28 h.


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