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. 1990 Dec;56(12):3755–3759. doi: 10.1128/aem.56.12.3755-3759.1990

Pectin Lyase Activity in a Penicillium italicum Strain

Aitor Alaña 1,†,*, Itziar Alkorta 1, Juan B Domínguez 1,‡, Maria J Llama 1, Juan L Serra 1
PMCID: PMC185063  PMID: 16348377

Abstract

An extracellular pectin lyase (PNL) [poly-(methoxygalacturonide)lyase; EC 4.2.2.10] produced by Penicillium italicum CECT 2294 grown on a surface bran (natural medium) or in a submerged (synthetic medium) culture was investigated. Both culture filtrates showed macerating activity at low pH on cucumber, potato, and orange tissues. The physicochemical properties of the enzyme obtained from both culture methods were identical, as well as its catalytic properties, which were assayed by different methods. The molecular mass of the PNL obtained by gel filtration chromatography was 22 kDa; the isoelectric point was 8.6, as determined by chromatofocusing; and the enzyme was able to catalyze the eliminative cleavage of pectins with low (37%) and high (from 54 to 82%) degrees of esterification. The PNL produced in liquid medium showed a Km for pectin (degree of esterification, 70%) of 3.2 mg/ml, and the optimum pH was 6.0 to 7.0. This enzyme was stable at 50°C and at pH 8.0. The ability of this PNL to macerate plant tissues in acidic environmental conditions, its stability at low pH and temperatures up to 50°C (thus preventing mesophilic microbial growth), and the absence of pectinesterase make this preparation useful for the food industry.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. ALBERSHEIM P., KILLIAS U. Studies relating to the purification and properties of pectin transeliminase. Arch Biochem Biophys. 1962 Apr;97:107–115. doi: 10.1016/0003-9861(62)90050-4. [DOI] [PubMed] [Google Scholar]
  2. Alaña A., Gabilondo A., Hernando F., Moragues M. D., Dominguez J. B., Llama M. J., Serra J. L. Pectin Lyase Production by a Penicillium italicum Strain. Appl Environ Microbiol. 1989 Jun;55(6):1612–1616. doi: 10.1128/aem.55.6.1612-1616.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Albersheim P. Auxin Induced Product Inhibition of Pectin Transeliminase as Shown by Ozonolysis. Plant Physiol. 1963 Jul;38(4):426–429. doi: 10.1104/pp.38.4.426. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Asahi M., Lindquist R., Fukuyama K., Apodaca G., Epstein W. L., McKerrow J. H. Purification and characterization of major extracellular proteinases from Trichophyton rubrum. Biochem J. 1985 Nov 15;232(1):139–144. doi: 10.1042/bj2320139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72:248–254. doi: 10.1016/0003-2697(76)90527-3. [DOI] [PubMed] [Google Scholar]
  6. Rexová-Benková L., Markovic O. Pectic enzymes. Adv Carbohydr Chem Biochem. 1976;33:323–385. doi: 10.1016/s0065-2318(08)60285-1. [DOI] [PubMed] [Google Scholar]
  7. SMOGYI M. Notes on sugar determination. J Biol Chem. 1952 Mar;195(1):19–23. [PubMed] [Google Scholar]

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