Studies on the effect of pH and carbon sources on enzyme activities of some pectinolytic bacteria isolated from jute retting water

The effect of pH of the assay media and different carbon sources in the culture media on the activities of 4 different enzymes, namely polygalacturonase (PG), pectin lyase (PNL), xylanase, and cellulase, of some pectinolytic bacteria were studied. The pectinolytic bacterial strains were isolated from the jute retting water bodies of 2 important jute growing areas of North 24 Parganas, West Bengal, India. The highest PG (12.45 to 41.0 IU/g cell wet weight) and PNL (22.55 to 75.7 U/mL) activities occurred at the alkaline pH of 8.0 and 8.5, respectively. Maximum xylanase activity (0.01 to 0.735 mmol/mL/min) occurred at pH 7.0. An acidic pH of 5.0 favored the cellulase activity (0 to 0.168 mmol/mL/min). All the enzymes were highly substrate specific and inducible in nature. The highest PG and PNL activities were observed in the presence of pectin, whereas the highest xylanase and cellulase activities were detected in the presence of xylan and cellulose, respectively, as the sole carbon source in the media.

Studies on the effect of pH and carbon sources on enzyme activities of some pectinolytic bacteria isolated from jute retting water

The effect of pH of the assay media and different carbon sources in the culture media on the activities of 4 different enzymes, namely polygalacturonase (PG), pectin lyase (PNL), xylanase, and cellulase, of some pectinolytic bacteria were studied. The pectinolytic bacterial strains were isolated from the jute retting water bodies of 2 important jute growing areas of North 24 Parganas, West Bengal, India. The highest PG (12.45 to 41.0 IU/g cell wet weight) and PNL (22.55 to 75.7 U/mL) activities occurred at the alkaline pH of 8.0 and 8.5, respectively. Maximum xylanase activity (0.01 to 0.735 mmol/mL/min) occurred at pH 7.0. An acidic pH of 5.0 favored the cellulase activity (0 to 0.168 mmol/mL/min). All the enzymes were highly substrate specific and inducible in nature. The highest PG and PNL activities were observed in the presence of pectin, whereas the highest xylanase and cellulase activities were detected in the presence of xylan and cellulose, respectively, as the sole carbon source in the media.

___

  • Jarman CG. Retting by traditional method. In: Th e retting of jute. Food and Agriculture Organization of the United Nations, Rome; 1985: pp. 11-22.
  • Banerjee B. Jute: especially as Produced in West Bengal. Economic Botany 9: 151-174, 1955.
  • Haque MS, Zakaria A, Adhir KB et al. Identifi cation of Micrococcus sp. responsible for the acceleration of jute retting. Pak J Biol Sci 6: 686-687, 2003. 4. Munshi TK, Chattoo BB. Bacterial population structure of the jute-retting environment. Microb Ecol 56: 270-282, 2008. 5. Zhang J, Henriksson G, Johansson G. Polygalacturonase is the key component in enzymatic retting of fl ax. J Biotechnol 81: 85-89, 2000.
  • Soriano M, Diaz P, Pastor FIJ. Pectinolytic systems of two aerobic sporogenous bacterial strains with high activity on pectin. Curr Microbiol 50: 114-118, 2005. 7. Haque MS, Asaduzzaman M, Alam S et al. Upgradation of SMR and seed-cut low grade barky jute fi bre through the application of fungi. Bangladesh J Jute Fib Res 14: 53-58, 1989.
  • Gomes I, Saha RK, Mohiuddin G et al. Isolation and characterization of a cellulase-free pectinolytic and hemicellulolytic thermophilic fungus. World J Microbiol Biotechnol 8: 589-592, 1992. 9. Voet D, Voet JG. Rates of enzymatic reactions. In: Biochemistry. 2nd ed. John Wiley & Sons, Inc; 1995: pp. 360-362.
  • Ahmed Z, Akhter F. Jute retting: an overview. Online J Biol Sci 1: 685-688, 2001.
  • Sambrook J, Russel DW. Molecular cloning: a laboratory manual. CSH Laboratory Press, Cold Spring Harbor, New York, 2001.
  • Kobayashi T, Higaki N, Suzumatsu A et al. Purifi cation and properties of a high-molecular-weight, alkaline exopolygalacturonase from a strain of Bacillus. Enzyme Microb Tech 29: 70-75, 2001.
  • Pitt D. Pectin lyase from Phoma medicaginis var. pinodella. Meth Enzymol 161: 350-365, 1988.
  • Bailey MJ, Biely P, Poutanen K. Interlaboratory testing of method for assay of xylanase activity. J Biotechnol 23: 257-270, 1992.
  • Miller GL, Blum R, Glennon WE et al. Measurement of carboxymethylcellulase activity. Anal Biochem 2: 127-132, 1960.
  • Tamburini E, Leon AG, Perito B et al. Characterization of bacterial pectinolytic strains involved in the water retting process. Environ Microbiol 5: 730-736, 2003.
  • Hoondal GS, Tiwari RP, Tewari R et al. Microbial alkaline pectinases and their industrial applications: a review. Appl Microbiol Biotechnol 59: 409-418, 2002.
  • Yadav S, Yadav PK, Yadav D et al. Pectin lyase: a review. Process Biochem 44: 1-10, 2009.
  • Kashyap DR, Chandra S, Kaul A et al. Production, purifi cation and characterization of pectinase from a Bacillus sp. DT7. World J Microbiol Biotechnol 16: 277-282, 2000.
  • Subramaniyan S, Prema P, Ramakrishna SV. Isolation and screening for alkaline thermostable xylanases. J Basic Microbiol 37: 431-437, 1997.
  • Annamalai N, Th avasi R, Jayalakshmi S et al. Th ermostable and alkaline tolerant xylanase production by Bacillus subtilis isolated from marine environment. Indian J Biotechnol 8: 291- 297, 2009.
  • Nakamura S, Nakai R, Wakabayashi K et al. Th ermophilic alkaline xylanase from newly isolated alkaliphilic and thermophilic Bacillus sp. strain TAR-1. Biosci Biotech Biochem 58: 78-81, 1994.
  • Lee SM, Koo YM. Pilot-scale production of cellulose using Trichoderma reesei Rut C-30 in fed-batch mode. J Microbiol Biotechnol 11: 229-233, 2001.
Turkish Journal of Biology-Cover
  • ISSN: 1300-0152
  • Yayın Aralığı: Yılda 6 Sayı
  • Yayıncı: TÜBİTAK
Sayıdaki Diğer Makaleler

Bioassay studies of 2'-O-ethylmurrangatin isolated from a medicinal plant, Murraya paniculata

Azizuddin SHAIKH, Muhammad İqbal CHOUDHARY

Production, purification, and characterization of a-amylase by Bacillus subtilis and its mutant derivates

Elif DEMİRKAN

Utilization of cytochrome oxidase I in Cephus pygmeus (L.) (Hymenoptera: Cephidae)

Ertan Mahir KORKMAZ, Mahir BUDAK, Hasan Hüseyin BAŞIBÜYÜK

Detection of prokaryotic microbial communities of Çamaltı Saltern, Turkey, by fluorescein in situ hybridization and real-time PCR

Mehmet Burçin MUTLU, Kıymet GÜVEN

The optimization of aDNA extraction protocol and sex determination of Bronze Age individuals from Oylum Höyük (Kilis, Turkey)

Serdal ARSLAN, Ayşen AÇIKKOL, Ertan Mahir KORKMAZ

Bioassay studies of 2ʹ-O-ethylmurrangatin isolated from a medicinal plant, Murraya paniculata

Azizuddin SHAIKH, Muhammad Iqbal CHOUDHARY

Production, purification, and characterization of α-amylase by Bacillus subtilis and its mutant derivates

Elif DEMİRKAN

Production of a novel bifunctional catalase-phenol oxidase of Scytalidium thermophilum in the presence of phenolic compounds

Yonca YÜZÜGÜLLÜ, Zümrüt Begüm ÖGEL, Ufuk Bakir BÖLÜKBAŞI, Nursen ÇORUH, Gürkan KARAKAŞ

Indirect somatic embryogenesis and shoot organogenesis from cotyledonary leaf segments of Digitalis lamarckii Ivan., an endemic medicinal species

Sandeep Kumar VERMA, Bahtiyar Buhara YÜCESAN, Songül GÜREL, Ekrem GÜREL

Investigation of Legionella pneumophila and free living amoebas in the domestic hot water systems in İstanbul

Dilara Meryem BURAK, Zuhal ZEYBEK