Protopectinase production in solid state culture ofAspergillus awamori |
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Authors: | Roque A Hours Takuo Sakai |
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Institution: | (1) Center for Research and Development of Bioresources, University of Osaka Prefecture, Gakuen cho 1-2, 593 Sakai City, Osaka, Japan;(2) Present address: Research and Development Center for Industrial Fermentations (CINDEFI), Faculty of Science, La Plata National University, 47 y 115, 1900 La Plata, Argentina |
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Abstract: | Summary Protopectinases (PPases) are a heterogeneous group of enzymes that release water soluble pectin from insoluble protopectin
in plant tissues by restricted degradation of the substrate. In all cases reported to date, PPases of bacterial or yeast origin
were produced in liquid culture. Here, we describe the growth and PPase production ofAspergillus awamori IFO 4033 in solid state culture.
Petri dishes containing 10 g of wheat bran and 15 ml of 0.2 M HCl were inoculated with 2 ml of a suspension with 1 × 105 spores.ml−1 and incubated for 48 h at 30°C. PPase activity on lemon (PPase-l) and apple (PPase-a) protopectins was maximum at 24 h of
culture (1490 and 610 U.g−1, respectively) and then decreased. Pectinase activity on lemon and apple pectin and polygalacturonase activity were maximum
at 48 h. Hence, the crude enzyme pool obtained at 24 h of process was appropriate for extraction of citrus and apple pectin
with a minor subsequent degradation of the solubilized pectin. The ratio of PPase-l to PPase-a changed during culture, so
there seemed to be at least two PPases with different substrate specificity. |
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