Summary
The strain SES28 was isolated from an indoor contaminated agar plate during a screening program for alkaliphilic CM-cellulose-degrading bacteria. It showed a prominent clear hydrolysis of the substrate at pH 10. The 16S rDNA analysis related it to the genus Nocardiopsis . Nocardiopsis sp. SES28 was able to grow at pH values up to 10.5, the major biomass being produced at pH 10, and pH 8 was the optimum for β-1,4-glucanase production. The optimum pH for β-1,4-glucanase activity was 9.0, and it was higher than 60% throughout the pH range 6.5–10.0; showing 94% of its a relative activity at pH 10. The feature of this bacterium to produce β-1,4-glucanase active in a broad pH-range might be useful for detergent- and textile-processing technologies.
References
Andersson A.M., Weiss N., Rainey F., Salkinoja-Salonen M.S., 1999 Dust-borne bacteria in animal sheds, schools and children’s day care centres Journal of Applied Microbiology 86: 622–634
Breccia J.D., Castro G.R., Baigorí M.D., Siñeriz F., 1995 Detection of endo-xylanase activities in electrophoretic gels with congo red staining Biotechnology techniques 9: 145–148
Cavalcanti M.T.H., Teixeira M.F.S., Filho J.L.L., Porto A.L.F., 2004 Partial purification of new milk-clotting enzyme produced by Nocardiopsis sp. Bioresource Technology 93: 29–35
Martinez M.A., Delgado O.D., Breccia J.D., Baigori M.D., Siñeriz F., 2002 Revision on taxonomic position of the xylanolytic Bacillus sp. MIR32 strain reidentified as Bacillus halodurans and plasmid mediated transformation of B. halodurans species Extremophiles 6: 391–395
Miller G.L., 1959 Use of dinitrosalicylic acid reagent for determination of reducing sugars Analytical Chemistry 31: 426–428
Mitsuiki S., Sakai M., Moriyama Y., Goto M., Furukawa K., 2002 Purification and some properties of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp TOA-1 Bioscience Biotechnology and Biochemistry 66: 164–167
Mitsuiki S., Ichikawa M., Oka T., Sakai M., Moriyama Y., Sameshima Y., Goto M., Furukawa K., 2004 Molecular characterization of a keratinolytic enzyme from an alkaliphilic Nocardiopsis sp. TOA-1 Enzyme and Microbial Technology 34: 482–489
Mordarska H., Zakrzewska-Czerwinska J., Pasciak M., Szponar B., Rowinski S., 1998 Rare, suppurative pulmonary infection caused by Nocardiopsis dassonvillei recognized by glycolipid markers FEMS Immunology and Medical Microbiology 21: 47–55
Navarrete-Bolanos J.L., Jimenez-Islas H., Botello-Alvarez E., Rico-Martinez R., Paredes-Lopez O., 2004 Improving xanthophyll extraction from marigold flower using cellulolytic enzymes Journal of Agricultural and Food Chemistry 52: 3394–3398
Pyc R., Sojka-Ledakowicz J., Bratkowska H., 2003 Biosynthesis of enzymes by Aspergillus niger IBT-90 and an evaluation of their application in textile technologies Fibres and Textiles Eastern Europe 11: 71–77
Rees H.C., Grant S., Jones B., Grant W.D., Heaphy S., 2003 Detecting cellulase and esterase enzyme activities encoded by novel genes present in environmental DNA libraries Extremophiles 7: 415–421
Shin J., Seo Y., Lee H.S., Rho J.R., Mo S.J., 2003 A new cyclic peptide from a marine-derived bacterium of the genus Nocardiopsis Journal of Natural Products 66: 883–884
Acknowledgements
This work was supported by CONICET (PEI 6166, PIP6205). Fundación Antorchas. Agregaduría Científica de la Embajada de Italia en Argentina.
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Walker, D., Ledesma, P., Delgado, O. et al. High endo-β-1,4-d-glucanase activity in a broad pH range from the alkali-tolerant Nocardiopsis sp. SES28. World J Microbiol Biotechnol 22, 761–764 (2006). https://doi.org/10.1007/s11274-005-9097-x
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DOI: https://doi.org/10.1007/s11274-005-9097-x