Screening for rhodanese producing Bacterium in freshly pressed Cassava effluents of a Cassava processing industry channeled to Odo-Oba Stream in Ogbomoso-Nigeria
Article Main
Abstract
Rhodanese is a key enzyme that plays an important role in cyanide detoxification. The enzyme was extracted, purified and physico-chemically characterised from Bacillus licheniformis which demonstrated the highest efficacy compared to the seven isolates of bacteria of the cassava processing industry effluent morpholologically and biochemically characterised. Statistical analysis was performed using one-way ANOVA and values were considered significant at p<0.05. This study showed that the optimum growth temperature was 350C at a pH 9.0. The highest duration time for the synthesis of rhodanese was at 40 hours. Potassium cyanide (KCN) and casein were the best carbon and nitrogen sources. The enzyme has a specific activity of 10.99 RU/mg, with a purification fold of 4.38, a percentage yield of 15.96%. The apparent Km for KCN and Sodium thiosulphate (Na2S2O3) were determined to be 30.24mM and 24.93mM respectively while their Vmax were 5.40 RU /ml/min and 5.07 RU /ml/min respectively. The optimum pH and temperature were 8.0 and 50 0C respectively. The enzyme showed a high stability at 500C. The enzyme showed specificity at 6.78 RU/ml/min for Na2S2O3 while it was inhibited by other sulphur containing substrates namely 2-mercaptoethanol, ammonium persulphate, and sodium metabisulphite The enzyme activity was not inhibited by metal ions such as (K+, Mg2+, Ba2+, Ni2+, Sn2+ and Na+) at 1mM and 10mM and was not significant (p>0.05). Therefore, B. licheniformis have the potentials of reducing cyanide pollution thereby enhancing effective management of cassava mill effluent before eventual discharge into the environment and this may be developed into a more effective tool for bioremediation.
Article Details
Article Details
Keywords
Bacillus licheniformis, Cassava, Effluent, Rhodanase
References
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Boey, C., Yeoh, H. and Chew M. (1976) Purification of tapioca leaf rhodanese. Phytochemistry, 15: 1343–1344.
Bradford, M. (1976) A Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72,248-254.
Chae MS, Schraft M, Hansen LT and Mackereth (2006). Effects of physiochemical surface chemical of listeria monocyogenis strain on attachment to glass. Food microbiology 23; 250-259.
Chew, M. Y. and Boey, C. G. (1972). Rhodanese of Tapioca leaf. Phytochemistry, 11,167 – 169.
Cosby, E. Q. and Summer, J. B. (1945) Rhodanese. Arch. Biochem. 7, 457-460.
Daramola, B. and S.A. Osanyinlusi, 2006. Investigation on modification of cassava starch using active components of ginger roots zingiber officinale roscoe. Afr. J. Biotechnol., 4: 1117-1123.
Dash, R.R., Gaur, A. and Balomajumder C. (2009). Cyanide in industrial wastewater and its removal: A review on biotreatment. Journal of Hazardous Materials 163: 1-11.
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Goyal K, Walton LJ, Tunnacliffe A (2005). Protien prevent protein aggregation due to water stress. Biochemical journal 388, 151-157.
Himwich, W. A. and Saunders, J. B. (1948). “Enzymic conversion of cyanide to thiocyanate,” American Journal of Physiology, vol. 53, pp. 348–354.
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Lovasoa Christine Razanamahandry, Hela Karoui, Harinaivo Anderson Andrianisa and Hamma Yacouba (2017). Bioremediation of soil and water polluted by cyanide: A review. Vol. 11(6), pp. 272-291. DOI: 10.5897/AJEST2016.2264
Lee, C. H., Hwang, J. H., Lee, Y. S. and Cho, K. S. (1995) “Purification and characterization of mouse liver rhodanese,” Journal of Biochemistry and Molecular Biology, vol. 28, pp. 170–176.
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O’Hair SK (1995). New crop fact sheet: Cassava [Online]. http://www.hort.purdue.edu/newcrop/cropfactsheets/cassava.html# Crop%20Culture%20(Agronomy/Horticulture) (August 30, 2008)
Oboh, G. and A.A. Akindahunsi and A.A. Oshodi, (2002). Nutrient and antinutrient content of Aspergillus nigerfermented cassava products flour and garri. J. Food Compo. Anal., 15: 617-622.
Oboh, G. and A.A. Akindahunsi, (2003). Chemical changes in cassava peels fermented with mixed cultured of Aspergillus niger and two species of Lactobacillus integrated Bio-system. Applied Trop. Agric., 8: 63-68.
Oboh, G., 2005. Isolation and characterization of amylase from fermented cassava (Manihot esculenta Crantz) wastewater. Afr. J. Biotechnol., 4: 1117-1123.
Okafor, N., 1998. An integrated bio-system for the disposal of cassava wastes. Proceedings of the Internet Conference on Integrated Bio-System in Zero Emission Applications.
Okonji RE, Fagbohunka BS, Ehigie LO, Ayinla AZ, Ojo OO. (2017. )Physicochemical properties of Rhodanese: A cyanide detoxifying enzyme from C (Baill) root. African Journal of Biotechnology. 16(14):704-711.
Okonji, R. E., Adewole, H. A., Kuku, A., and Agboola, F.K. (2011).Physicochemical properties of Mudskipper (periophthalamus barbarous pallas) liver rhodanese. Australian journal of basic and applied sciences
Oluwatosin A.A., Aladesanmi O, Funakinwa O RE Okonji (2017). Bioeffiency of indigenous microbial rhodanase in cleanup of cyanide containminated stream in Modakeke, Ile-Ife, Nigeria. Journal of bioremediation and biodegradation. Vol: 8, issue ;390.
Oyedeji Olaoluwa, Kehinde O. Awojobi, Raphael E. Okonji and Olufemi O. Olusola (2013). Characterization of rhodanese produced by Pseudomonas aeruginosa and Bacillus brevis isolated from soil of cassava processing site. African Journal of Biotechnology Vol. 12(10), pp. 1104-1114. Available online at http://www.academicjournals.org/AJB DOI: 10.5897/AJB12.2241 ISSN 1684–5315
Panos NH, Bellini MR (1999). Microbial degradation of cyanides. Mine, water and environment. 1; 201-206.
Raimbault, M., 1998. General and microbiology aspect of solid substrate fermentation. Elect. J. Biotechnol, 1: 26-27.
Saidu Y (2005). Comparative rhodanase activity in liver and breast muscles od some avian species. Bulletin of SAN vol. 26 (2005). 494-498
Sorbo BH (1951) On the Properties of Rhodanese: Partial 3urification, Inhibitors and Intracellular distribution. Acta Chemical Scandinavia 5: 724-726
Sorbo, B. H. (1953b). Crystalline Rhodanese. Enzyme catalyzed reaction. Acta Chemical Scandinavia 7: 1137-1145.
Westley J, Adler H, Westley L, Nishido C (1983). The Sulphur transferases. Fundamental Applied Toxicology 3:337-382.
Akinsiku, O. T., Agboola, F. K., Kuku, A. and Afolayan, A. (2010). Physicochemical and kinetic characteristics of rhodanese from the liver of African catfish Clarias gariepinus Burchell in Asejire lake, Fish Physiology and Biochemistry, 36 (3): 573–586.
Banerjee, R. & Bhattacharyya, B.C. Biotechnol Lett (1992) 14: 301. https://doi.org/10.1007/BF01022328
Boey, C., Yeoh, H. and Chew M. (1976) Purification of tapioca leaf rhodanese. Phytochemistry, 15: 1343–1344.
Bradford, M. (1976) A Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72,248-254.
Chae MS, Schraft M, Hansen LT and Mackereth (2006). Effects of physiochemical surface chemical of listeria monocyogenis strain on attachment to glass. Food microbiology 23; 250-259.
Chew, M. Y. and Boey, C. G. (1972). Rhodanese of Tapioca leaf. Phytochemistry, 11,167 – 169.
Cosby, E. Q. and Summer, J. B. (1945) Rhodanese. Arch. Biochem. 7, 457-460.
Daramola, B. and S.A. Osanyinlusi, 2006. Investigation on modification of cassava starch using active components of ginger roots zingiber officinale roscoe. Afr. J. Biotechnol., 4: 1117-1123.
Dash, R.R., Gaur, A. and Balomajumder C. (2009). Cyanide in industrial wastewater and its removal: A review on biotreatment. Journal of Hazardous Materials 163: 1-11.
Domenico, B., Daniela, D., Rita, C., Aristodemo, C., Silvia, P., and Martino, B. (2000). The crystal structure of a sulphur transferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzymes families. Journal of Molecular Biology 298 (4): 691 – 704.
Ehigie AF, Abdulrasak MA, Adeleke GE, Ehigie OL (2019) Comparison of Rhodanese Activity and Distribution in Tomato (Solanum lycopersicum Mill.) Plant Parts and its Physicochemical Characterization. J Plant Biochem Physiol. 7:240
Ehigie O. L., Okonji R. E., Balogun R. O. and K.D.S. Bamitale (2013). Distribution of Enzyme (Rhodanese, 3-Mercaptopyruvate Sulphurtransferase, Arginase And Thiaminase) in Some Commonly Consumed Plant Tubers in Nigeria. Innovative Systems Design and Engineering vol.4, No.9, pp.7-14.
Ehigie Ona Leonard, Okonji Raphael Emuebie and Mohammed Adewumi Abdulrasak. (2016). Kinetics and biochemical characterization of Rhodanase from seed, mesocarp and capsule of Snake tomato (Trichosanthes cucumerina). www.Actaverlit.com. ISSN: 2394-3092, Vol (4) issue (3). Page 9-37
Fagbohunka K. and Okonji, R. E. (2004). “Presence of rhodanese in the cytosolic fraction of the fruit bat (Eidolon helvum) liver,” Journal of Biochemistry and Molecular Biology, 37 (3): 275–281.
Goyal K, Walton LJ, Tunnacliffe A (2005). Protien prevent protein aggregation due to water stress. Biochemical journal 388, 151-157.
Himwich, W. A. and Saunders, J. B. (1948). “Enzymic conversion of cyanide to thiocyanate,” American Journal of Physiology, vol. 53, pp. 348–354.
Holt JG, Krieg NR, Sneath PHA, Staley JT, Williams ST (1994) Bergey’sManual of Determinative Bacteriology. Williams & Wilkins, Baltimore, Baltimore, Maryland, USA
Itakorode BO, Okonji E, Adedeji O, Torimiro N, Onwudiegwu C, Oluwaseyi A.(2019). Studies on some physicochemical properties of Rhodanese synthesized by B. cereus isolated from the effluents of iron and steel smelting industry. African Journal of Biochemistry Research.;13(1):1-8.
Iyayi, E.A. and D.M. Losel, 2001. Changes in carbohydrate fractions of cassava peels following fungal solid state fermentation. J. Food Technol. Afr., 6: 101-103.
Kumar CG Takagi H (1999). Microbial alkaline protease from a bio-industial viewpoint Biotechnonolgy Adv. 15; 17 (7); 1-94.
Lovasoa Christine Razanamahandry, Hela Karoui, Harinaivo Anderson Andrianisa and Hamma Yacouba (2017). Bioremediation of soil and water polluted by cyanide: A review. Vol. 11(6), pp. 272-291. DOI: 10.5897/AJEST2016.2264
Lee, C. H., Hwang, J. H., Lee, Y. S. and Cho, K. S. (1995) “Purification and characterization of mouse liver rhodanese,” Journal of Biochemistry and Molecular Biology, vol. 28, pp. 170–176.
Lineweaver, H. and Burk, D.(1934) The Determination of Enzyme Dissociation Constants. Journal of American Chemical Society’ 56, 658.
O’Hair SK (1995). New crop fact sheet: Cassava [Online]. http://www.hort.purdue.edu/newcrop/cropfactsheets/cassava.html# Crop%20Culture%20(Agronomy/Horticulture) (August 30, 2008)
Oboh, G. and A.A. Akindahunsi and A.A. Oshodi, (2002). Nutrient and antinutrient content of Aspergillus nigerfermented cassava products flour and garri. J. Food Compo. Anal., 15: 617-622.
Oboh, G. and A.A. Akindahunsi, (2003). Chemical changes in cassava peels fermented with mixed cultured of Aspergillus niger and two species of Lactobacillus integrated Bio-system. Applied Trop. Agric., 8: 63-68.
Oboh, G., 2005. Isolation and characterization of amylase from fermented cassava (Manihot esculenta Crantz) wastewater. Afr. J. Biotechnol., 4: 1117-1123.
Okafor, N., 1998. An integrated bio-system for the disposal of cassava wastes. Proceedings of the Internet Conference on Integrated Bio-System in Zero Emission Applications.
Okonji RE, Fagbohunka BS, Ehigie LO, Ayinla AZ, Ojo OO. (2017. )Physicochemical properties of Rhodanese: A cyanide detoxifying enzyme from C (Baill) root. African Journal of Biotechnology. 16(14):704-711.
Okonji, R. E., Adewole, H. A., Kuku, A., and Agboola, F.K. (2011).Physicochemical properties of Mudskipper (periophthalamus barbarous pallas) liver rhodanese. Australian journal of basic and applied sciences
Oluwatosin A.A., Aladesanmi O, Funakinwa O RE Okonji (2017). Bioeffiency of indigenous microbial rhodanase in cleanup of cyanide containminated stream in Modakeke, Ile-Ife, Nigeria. Journal of bioremediation and biodegradation. Vol: 8, issue ;390.
Oyedeji Olaoluwa, Kehinde O. Awojobi, Raphael E. Okonji and Olufemi O. Olusola (2013). Characterization of rhodanese produced by Pseudomonas aeruginosa and Bacillus brevis isolated from soil of cassava processing site. African Journal of Biotechnology Vol. 12(10), pp. 1104-1114. Available online at http://www.academicjournals.org/AJB DOI: 10.5897/AJB12.2241 ISSN 1684–5315
Panos NH, Bellini MR (1999). Microbial degradation of cyanides. Mine, water and environment. 1; 201-206.
Raimbault, M., 1998. General and microbiology aspect of solid substrate fermentation. Elect. J. Biotechnol, 1: 26-27.
Saidu Y (2005). Comparative rhodanase activity in liver and breast muscles od some avian species. Bulletin of SAN vol. 26 (2005). 494-498
Sorbo BH (1951) On the Properties of Rhodanese: Partial 3urification, Inhibitors and Intracellular distribution. Acta Chemical Scandinavia 5: 724-726
Sorbo, B. H. (1953b). Crystalline Rhodanese. Enzyme catalyzed reaction. Acta Chemical Scandinavia 7: 1137-1145.
Westley J, Adler H, Westley L, Nishido C (1983). The Sulphur transferases. Fundamental Applied Toxicology 3:337-382.
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Screening for rhodanese producing Bacterium in freshly pressed Cassava effluents of a Cassava processing industry channeled to Odo-Oba Stream in Ogbomoso-Nigeria. (2019). Journal of Applied and Natural Science, 11(3), 650-656. https://doi.org/10.31018/jans.v11i3.2055
