Pectinase Production by Bacillus and Paenibacillus sp. Isolated from Decomposing Wood Residues in the Lagos Lagoon

Authors

  • Busayo Tosin Akinyemi University of Lagos
  • Olanike Maria Buraimoh UNIVERSITY OF LAGOS
  • Olayemi Omowunmi Ogunrinde UNIVERSITY OF LAGOS
  • Olukayode Oladipo Amund UNIVERSITY OF LAGOS

DOI:

https://doi.org/10.11594/jtls.07.03.03

Keywords:

Pectinase, Peanibacillus sp., Bacillus megaterium, Bacillus bataviensis

Abstract

Three wood decomposing bacteria isolated from the Lagos lagoon, Bacillus megaterium, Bacillus bataviensis and Paenibacillus sp. were screened for their pectinase producing abilities using pectin as substrate under submerged fermentation (SMF) conditions. The results showed that all three isolates produced appreciable pectinolytic activities. Paenibacillus sp. showed the highest pectinase activity when compared with the other two isolates. The optimum pH for pectinase activity for both B. megaterium and B. bataviensis was 8.0 while it was 6.5 for Paenibacillus sp., B. bataviensis, and B. megaterium showed optimum pectinase activity at 60°C and Paenibacillus sp. at 40°C. Metal ions such as Na+ and K+ improved the activity of pectinase produced by the three isolates when compared to the effect of Zn2+ and Mn2+. The molecular weights of the enzymes were also estimated by gel filtration as 29,512 da, 32,359 da, and 25,119 da for Paenibacillus sp., B. megaterium and B. bataviensis respectively. The study has provided a platform for further investigation into the biochemical characterization of the enzyme, and optimization of culture conditions to scale up pectinase production for commercial exploitation.

Author Biographies

Busayo Tosin Akinyemi, University of Lagos

MICROBIOLOGY, GRADUATE ASSISTANT

Olanike Maria Buraimoh, UNIVERSITY OF LAGOS

MICROBIOLOGY, LECTURER II

Olayemi Omowunmi Ogunrinde, UNIVERSITY OF LAGOS

MICROBIOLOGY, POSTGRADUATE (MSC)

Olukayode Oladipo Amund, UNIVERSITY OF LAGOS

MICROBIOLOGY, PROFESSOR

References

Voragen AGJ, Coenen G, Verhoef RP, Schols HA (2009) Pectin, a versatile polysaccharide present in plant cell walls. Structural Chemistry 20: 263 – 275. doi: 10.1007/s11224-009-9442-z.

Kapoor M, Beg QK, Bhushan B et al. (2001) Application of alkaline and thermostable polygalacturonase from Bacillus spp. MG-cp-2 in degumming of ramie (Boehmeria nivea) and sunn hemp (Crotolaria juncia) bast fibres. Process Biochemistry 36 (8 – 9): 803 – 807. doi: 10.1016/S0032-9592(00)00282-X.

Kaur G, Kumar S, Satyanarayana T (2004) Production, characterization and application of a thermostable polyga-lacturonase of a thermophilic mould sporotrichum thermophile Apinis. Bioresource Technology 94 (3): 239 – 243. doi: 10.1016/j.biortech.2003.05.003.

Vibha B, Neelam G (2010) Exploitation of microorganisms for screening of pectinase from environment. In Proceedings of 8th International Conference Globelics: 1 – 3 November 2010; Kuala Lumpur.

Jacob N, Poorna AC, Prema P (2008) Purification and partial characterization of polygalacturonase from Steptomyces lydicus. Bioresource Technology 99 (14): 6697 – 6701. doi: 10.1016/j.biortech.2007.10.002.

Sunnotel O, Nigam P (2002) Pectinolytic activity of bacteria isolated from soil and two fungal strains during sub-merged fermentation. World Journal of Microbiology and Biotechnology 18 (9): 835 – 839. doi: 10.1023/A:1021209123641.

Buraimoh OM, Ilori MO, Amund OO et al. (2015) Assessment of bacterial degradation of lignocellulosic resi-dues (sawdust) in a tropical estuarine microcosm using improvise floating raft equipment. International Biodeterioration and Biodegradation 104:186 – 193. doi: 10.1016/j.ibiod.2015.06.010.

Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. Journal of Biological Chemistry 195: 265 – 275.

Nelson N (1944) A photometric adaptation of the Somogyi method for the determination of glucose. Journal of Biological Chemistry 153 (2): 375 – 380.

Somogyi M (1952) Notes on sugar determination. Journal of Biological Chemistry 195 (1): 19 – 23.

Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Analytical Chemistry 31(3): 426 – 428. doi: 10.1021/ac60147a030.

Stark E, Tetrault PA (1951) Isolation of cell-free starch saccharifying enzymes from the medium at 70oC. Journal of Bacteriology 62 (2): 247 – 252.

Soriano M, Diaz P, Pastor FIJ (2006) Pectinolytic systems of two aerobic sporogenous bacterial strains with high activity on pectin. Current Microbiology 50 (2): 114 – 118. doi: 10.1007/s00284-004-4382-8.

Yadav S, Yadav PK, Yadav D, Yadav KDS (2008) Purification and characterization of an alkaline pectin lyase from Aspergillus flavus. Process Biochemistry 43 (5): 547 – 555. doi: 10.1016/j.procbio.2008.01.015.

Torimiro N, Okonji RE (2013) A comparative study of pectinolytic enzyme production by Bacillus species. African Journal of Biotechnology 12 (46): 6498 – 6503. doi: 10.5897/AJB2013.12421.

Shweta RG, Khobragade CN, Shilpa GJ (2016) Extracellular pectinase activity from Bacillus cereus GC Subgroup A: Isolation, production, optimization and partial characterization. Journal of Microbiology, Biotechnology and Food Sciences 6 (2): 767 – 772.

Hirose N, Kishida M, Kawasaki H, Sakai T (1999) Purification and characterization of an endo-polygalacturonase from a mutant of Saccharomyces cerevisiae. Bioscience, Biotechnology, and Biochemistry. 63:1100-1103. doi: 10.1271/bbb.63.1100.

Downloads

Published

2017-09-11

Issue

Vol. 7 No. 3 (2017)

Section

Articles

License

The work has not been published before (except in the form of an abstract or part of a published lecture or thesis) and it is not under consideration for publication elsewhere. When the manuscript is accepted for publication in this journal, the authors agree to automatic transfer of the copyright to the publisher.

Creative Commons License
Journal of Tropical Life Science is licensed under Creative Commons Attribution-NonCommercial 4.0 International License