Pectinolytic enzymes secreted by yeasts from tropical fruits

Three hundred yeasts isolated from tropical fruits were screened in relation to secretion of pectinases. Twenty-one isolates were able to produce polygalacturonase and among them seven isolates could secrete pectin lyase. None of the isolates was able to secrete pectin methylesterase. The pectinolyt...

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Bibliographic Details
Published in:	FEMS yeast research Vol. 5; no. 9; pp. 859 - 865
Main Authors:	da Silva, Evânia Geralda, Borges, Maria de Fátima, Medina, Clara, Piccoli, Roberta Hilsdorf, Schwan, Rosane Freitas
Format:	Journal Article
Language:	English
Published:	Oxford, UK Elsevier B.V 01-06-2005 Blackwell Publishing Ltd Oxford University Press
Subjects:	Carboxylic Ester Hydrolases - isolation & purification Carboxylic Ester Hydrolases - metabolism Fruit - microbiology Fruits Hydrogen-Ion Concentration Kluyveromyces wickerhamii Pectin Pectin lyase Pectin lyases Pectinases Pectinesterase Pectinolytic enzymes Polygalacturonase Polygalacturonase - isolation & purification Polygalacturonase - metabolism Polygalacturonases Polysaccharide-Lyases - isolation & purification Polysaccharide-Lyases - metabolism Stephanoascus smithiae Tropical fruits Viscosity Yeast Yeasts - enzymology Pectinases Stephanoascus smithiae Kluyveromyces wickerhamii Tropical fruits Polygalacturonases Pectin lyases
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Summary:	Three hundred yeasts isolated from tropical fruits were screened in relation to secretion of pectinases. Twenty-one isolates were able to produce polygalacturonase and among them seven isolates could secrete pectin lyase. None of the isolates was able to secrete pectin methylesterase. The pectinolytic yeasts identified belonged to six different genera. Kluyveromyces wickerhamii isolated from the fruit mangaba ( Hancornia speciosa) secreted the highest amount of polygalacturonase, followed by K. marxianus and Stephanoascus smithiae. The yeast Debaryomyces hansenii produced the greatest decrease in viscosity while only 3% of the glycosidic linkages were hydrolysed, indicating that the enzyme secreted was an endo-polygalacturonase. The hydrolysis of pectin by polygalacturonase secreted by S. smithiae suggested an exo-splitting mechanism. The other yeast species studied showed low polygalacturonase activity.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	1567-1356 1567-1364
DOI:	10.1016/j.femsyr.2005.02.006