Properties of a Polygalacturonase Produced by Acrocylindrium

Kimura, Hitoshi; Uchino, Fuji; Mizushima, Shôji

doi:10.1099/00221287-74-1-127

Cited by 13 publications

(3 citation statements)

References 15 publications

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“…The organism was routinely grown and maintained on acidified-streptomycin potato dextrose agar slants at 40ºC as stock. The ability of the fungus to produce PME was ascertained by the methods of Kimural et al (1993) and Andro et al (1984). The medium contained pectin, 1 g; NH4NO3, 1 g; MgSO4.7H2O, 0.05 g; CaCl2.…”

Section: Organismmentioning

confidence: 99%

Purification and characterization of pectinmethylesterase from Aspergillus repens isolated from cultivated soil

Arotupin¹,

D²,

Akinyosoye³

et al. 2008

Afr. J. Biotechnol.

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Aspergillus repens isolated from cultivated soils released pectinmethylesterase (PME) into the liquid culture medium during growth. The enzyme preparation was partially purified by ammonium sulphate precipitation and dialysed. The ammonium sulphate-dialysate fraction of the enzyme was separated by molecular exclusion and ion exchange chromatography. The molecular weight of the enzyme was found to be 141,300 daltons. The optimum temperature for PME activity was 30 o C and most active at pH 6.5. The activity of the enzyme was stimulated by Na + , K + , Ca 2+ , Mg 2+ and Zn 2+ , while EDTA, PbCl 2 , HgCl 2 and IAA inhibited enzyme activity. The activity of the enzyme increased with increase in substrate concentration reaching maximum at 4 mg/ml. The Lineweaver-Burk plot for the hydrolysis of pectin indicated approximately 1.3 mg/ml. These qualities could be explored during the industrial applications of this enzyme.

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Section: Organismmentioning

confidence: 99%

Purification and characterization of pectinmethylesterase from Aspergillus repens isolated from cultivated soil

Arotupin¹,

D²,

Akinyosoye³

et al. 2008

Afr. J. Biotechnol.

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“…The organism was routinely grown and maintained according to Arotupin et al (2008). The prelimnary screening of the organism for elaboration of polygalcturonase (PG) was carried out with the method of Kimural et al (1993).…”

Section: Sources Of Organismsmentioning

confidence: 99%

Purification, Characterization and Application of Polygalacturonase from Aspergillus niger CSTRF

Arotupin¹,

Akinyosoye²,

Onifade³

2012

MJM

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Aims:The research was carried out to study the purification, characterization and application of polygalacturonase from Aspergillus niger CSTRF. Methodology and Results: The polygalacturonase (PG) from the fungus was purified by ammonium sulphate precipitation and dialysed. The resulting fraction of the enzyme was further separated by molecular exclusion and ion exchange chromatography. The enzyme was purified 28.19 fold with a yield of approximately 69 % following purification with SP C-50. It has a relative molecular weight of 79,430 daltons and markedly influenced by temperature, pH and substrate concentrations of reactions with optimum activity at 35 °C, pH 4.0 and 8 mg/mL respectively. The PG was heat stable over a broad range of temperatures. Line weaver-Burk plot for the apparent hydrolysis of pectin showed approximately Km value of 2.7 mg/mL. The activity of the enzyme was enhanced by Na + , Ca 2+ , Mg 2+ and Zn 2+ , while EDTA, PbCl2, HgCl2 and IAA were inhibitory. The ability of the purified enzyme to clarify fruit juice was also investigated. Conclusion, significance and impact of the study: This study revealed that polygalacturonase possesses properties for clarification of fruit juice and by extension bioprocessing applications.

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“…Endopolygalacturonase (endoPG) (EC 3.2.1.15), exopolygalacturonase (exoPG) (EC 3.2.1.15), and pectinesterase (PE) (EC 3.1.1.11) were induced simultaneously in a strain of Acrocylindrium grown on pectin as a carbon source (1)(2)(3). Therefore, a question arose whether the induction of these enzymes was under the same genetic control or not.…”

mentioning

confidence: 99%