Multiple Applications of Enzymes Induced by Algal Biomasses from a New Bacillus Isolate to Saccharify Algae and Degrade Chemical Dyes
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To find a multifunctional lignocellulolytic enzyme-producing strain, ten bacterial isolates from paper mill wastewater were tested for their carboxymethyl cellulose (CMC) hydrolytic ability. Bacillus sp. TPF-1, which exhibits the highest hydrolytic ability, was selected to produce lignocellulolytic enzymes using various biomass types as carbon sources. The highest CMCase (9.12 U/mL) and xylanase (102.55 U/mL) activities were obtained by green algae, and the maximum laccase activity (7037.28 U/L) was induced by Sargassum fusiforme. CMCase and xylanase showed the highest activities at 55 and 50 °C, respectively, with the same optimum pH of 5.4. The laccase exhibited optimum temperature of 40 °C and retained 60% more activity at 80 °C in extreme acid conditions (pH 2.2). To explore the multiple applications of these enzymes, crude enzymes induced by green algae were used to saccharify untreated algae. The reducing sugar produced by crude enzymes and commercial cellulase was 23 and 14% higher than that of the control, respectively, and it was 48% higher using crude enzymes with commercial cellulase (72 h). Additionally, the laccase induced by S. fusiforme was tested to decolorize two chemical dyes under an acidic condition (pH 2.2). The highest decolorization rates were 56.13 and 62.14% for Coomassie brilliant blue R-250 and Congo Red, respectively, in the presence of hydroxybenzotriazole monohydrate.
KeywordsBacillus CMCase Algae Laccase Xylanase
We acknowledge the financial support from BioFuelNet Canada, Lakehead University, National Special Fund for Forestry Scientific Research in the Public Interest of China (Grant No. 201504406), Natural Science Foundation of the Jiangsu Higher Education Institutions of China (Grant No. 15KJA220004), and Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD).
Compliance with Ethical Standards
Conflict of interest
No conflict of interest exits in the submission of this manuscript. We declare that we do not have any commercial or associative interest that represents a conflict of interest in the work submitted.
- 5.Otajevwo, F., Aluyi, H.: Cultural conditions necessary for optimal cellulase yield by cellulolytic bacterial organisms as they relate to residual sugars released in broth medium. Mod. Appl. Sci. 5(3), 141–151 (2011)Google Scholar
- 6.Daniel, G., Nilsson, T.: Developments in the study of soft rot and bacterial decay. In: Bruce, A., Palfreyman, J.W. (eds.) Forest Products Biotechnology, pp. 37–62. Taylor & Francis, London (1998)Google Scholar
- 7.Kim, H.-J., Lee, Y.-J., Gao, W., Chung, C.-H., Son, C.-W., Lee, J.-W.: Statistical optimization of fermentation conditions and comparison of their influences on production of cellulases by a psychrophilic marine bacterium, Psychrobacter aquimaris LBH-10 using orthogonal array method. Biotechnol. Bioprocess Eng. 16(3), 542–548 (2011)CrossRefGoogle Scholar
- 9.Hung, K.-S., Liu, S.-M., Tzou, W.-S., Lin, F.-P., Pan, C.-L., Fang, T.-Y., Sun, K.-H., Tang, S.-J.: Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1. Process Biochem. 46(6), 1257–1263 (2011)CrossRefGoogle Scholar
- 13.Givaudan, A., Effosse, A., Faure, D., Potier, P., Bouillant, M.-L., Bally, R.: Polyphenol oxidase in Azospirillum lipoferum isolated from rice rhizosphere: evidence for laccase activity in non-motile strains of Azospirillum lipoferum. FEMS Microbiol. Lett. 108(2), 205–210 (1993)CrossRefGoogle Scholar
- 22.Maki, M., Broere, M., Leung, K., Qin, W.: Characterization of some efficient cellulase producing bacteria isolated from paper mill sludges and organic fertilizers. Int. J. Biochem. Mol. Biol. 2(2), 146–154 (2011)Google Scholar
- 31.Martins, L.O., Soares, C.M., Pereira, M.M., Teixeira, M., Costa, T., Jones, G.H., Henriques, A.O.: Molecular and biochemical characterization of a highly stable bacterial laccase that occurs as a structural component of the Bacillus subtilis endospore coat. J. Biol. Chem. 277(21), 18849–18859 (2002)CrossRefGoogle Scholar
- 32.Kocabas, A., Kocabas, D.S., Bolukbasi, U.B.: One-Step purification and characterization of a low molecular weight xylanase from Aspergillus terreus NRRL 1960. J. Appl. Biol. Sci. 5(2), 61–65 (2011)Google Scholar
- 35.Panwar, D., Srivastava, P.K., Kapoor, M.: Production, extraction and characterization of alkaline xylanase from Bacillus sp. PKD-9 with potential for poultry feed. Biocatal. Agric. Biotechnol. 3(2), 118–125 (2014)Google Scholar
- 36.Amore, A., Parameswaran, B., Kumar, R., Birolo, L., Vinciguerra, R., Marcolongo, L., Ionata, E., La Cara, F., Pandey, A., Faraco, V.: Application of a new xylanase activity from Bacillus amyloliquefaciens XR44A in brewer’s spent grain saccharification. J. Chem. Technol. Biotechnol. 90(3), 573–581 (2015)CrossRefGoogle Scholar
- 38.Goyal, V., Mittal, A., Bhuwal, A.K., Singh, G., Yadav, A., Aggarwal, N.K.: Parametric optimization of cultural conditions for carboxymethyl cellulase production using pretreated rice straw by Bacillus sp. 313SI under stationary and shaking conditions. Biotechnol. Res. Int. 2014(12), 651839 (2014)Google Scholar
- 40.Ariffin, H., Abdullah, N., Kalsom, M.U., Shirai, Y., Hassan, M.: Production and characterisation of cellulase by Bacillus pumilus EB3. Int. J. Eng. Technol. 3(1), 47–53 (2006)Google Scholar