Production, partial purification and characterization of [alpha]-l-rhamnosidase from Penicillium ulaiense

Penicillium ulaiense is a post-harvest pathogenic fungus that attacks citrus fruits. The objective of this work was to study this microorganism as an α-l-rhamnosidase producer and to characterize it from P. ulaiense. The enzyme under study is used for different applications in food and beverage indu...

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Bibliographic Details
Published inWorld journal of microbiology & biotechnology Vol. 25; no. 6; pp. 1025 - 1033
Main Authors Rajal, Veronica Beatriz, Cid, Alicia Graciela, Ellenrieder, Guillermo, Cuevas, Carlos Mario
Format Journal Article
LanguageEnglish
Published Oxford Springer Nature B.V 01.06.2009
Subjects
Batch reactors
Carbon sources
Chemical products
Citrus
Citrus fruits
Cobalt
Design of experiments
Enzymes
Mycotoxins
Penicillium
Potassium
Studies
Vitaceae
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Summary:Penicillium ulaiense is a post-harvest pathogenic fungus that attacks citrus fruits. The objective of this work was to study this microorganism as an α-l-rhamnosidase producer and to characterize it from P. ulaiense. The enzyme under study is used for different applications in food and beverage industries. α-l-Rhamnosidase was produced in a stirred-batch reactor using rhamnose as the main carbon source. The kinetic parameters for the growth of the fungi and for the enzyme production were calculated from the experimental values. A method for partial purification, including (NH4)2SO4 precipitation, incubation at pH 12 and DEAE-sepharose chromatography yielded an enzyme with very low β-glucosidase activity. The pH and temperature optima were 5.0 and 60°C, respectively. The Michaelis-Menten constants for the hydrolysis of p-nitrophenyl-α-l-rhamnoside were Vmax = 26 ± 4 IU ml-1 and Km = 11 ± 2 mM. The enzyme showed good thermostability up to 60°C and good operational stability in white wine. Co2+ affected positively the activity; EDTA, Mn2+, Mg2+, dithiotreitol and Cu2+ reduced the activity by different amounts, and Hg2+ completely inhibited the enzyme. The enzyme showed more activity on p-nitrophenyl-α-l-rhamnoside than on naringin. According to these results, this enzyme has potential for use in the food and pharmacy industries since P. ulaiense does not produce mycotoxins. [PUBLICATION ABSTRACT]
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ISSN:0959-3993
1573-0972
DOI:10.1007/s11274-009-9979-4