Browse > Article

Pectolytic Enzymes of the Industrial Fungus Aspergillus kawachii  

Vita, Carolina Elena (CINDEFI (UNLP, CCT-La Plata, CONICET))
Esquivel, Juan Carlos Contreras (Laboratorio de Glicobiotecnologia Aplicada, Departamento de Investigacion en Alimentos, Facultad de Ciencias Quimicas, Universidad Autonoma de Coahuila)
Voget, Claudio Enrique (CINDEFI (UNLP, CCT-La Plata, CONICET))
Publication Information
Food Science and Biotechnology / v.18, no.6, 2009 , pp. 1365-1370 More about this Journal
Abstract
Aspergillus kawachii extracellular pectinases were screened in liquid cultures with different carbon sources. The fungus grown on citrus pectin or lemon pomace produced at least one of these inducible pectinases: acidic polygalacturonase, pectin lyase, pectin methylesterase, $\alpha$-L-arabinofuranosidase, $\alpha$-1,5-endoarabinase, $\beta$-D-galactosidase/exogalactanase, and $\beta$-1,4-endogalactanase. The lemon-pomace filtrates also contained significant $\alpha$-L-rhamnosidase and $\beta$-D-fucosidase activities. Most of the screened pectinases were active at pH 2.0-2.5, indicating that the A. kawachii enzymes were acidophilic. Under the culture conditions employed we could not detect enzymatic degradation of soybean rhamnogalacturonan. The A. kawachii pectinase-production-related regulatory phenomena of induction-repression resemble those described for other Aspergillus sp.
Keywords
Aspergillus kawachii; pectolytic enzymes; carbon source;
Citations & Related Records

Times Cited By Web Of Science : 1  (Related Records In Web of Science)
Times Cited By SCOPUS : 1
연도 인용수 순위
1 Iwashita K, Todoroki K, Kmura H, Shimoi H, Ito K. Purification and characterization of extracellular cell wall bound $\beta$-glucosidases from Aspergillus kawachii. Biosci. Biotech. Bioch. 62: 1938-1946 (1998)   DOI   ScienceOn
2 Kojima Y, Sakamoto T, Kishida M, Sakai T, Kawasaki H. Acid condition-inducible polygalacturonase of Aspergillus kawachii. J. Mol. Catal. B: Enzym. 6: 351-357 (1999)   DOI   ScienceOn
3 Contreras Esquivel JC, Voget CE. Purification and characterization of an acidic polygalacturonase from Aspergillus kawachii. J. Biotechnol. 110: 21-28 (2004)   DOI   ScienceOn
4 Voget CE, Vita CE, Contreras Esquivel JC. One-step concentration and partial purification of non-acidic Aspergillus kawachii polygalacturonases by adsorption to glass fiber microfilters. Biotechnol. Lett. 28: 233-239 (2006)   DOI   ScienceOn
5 Albersheim P. Pectin lyase from fungi. Vol. 8, pp. 628-631. In: Methods in Enzymology. Neufeld EF, Guinsburg V (eds). Academic Press, San Diego, CA, USA (1966)
6 Blumenkrantz N, Asboe-Hansen G. New method for quantitative determination of uronic acids. Anal. Biochem. 54: 484-489 (1973)   DOI   ScienceOn
7 Voragen AGJ, Beldman G, Schols H. Chemistry and enzymology of pectins. pp. 19-23. In: Advanced Dietary Fiber Technology. McCleary BV, Prosky L (eds). Blackwell Publishing, Oxford, UK (2001)
8 Ito K, Ogasawa H, Sugimoto T, Ishikawa T. Purification and properties of acid stable xylanases from Aspergillus kawachii. Biosci. Biotech. Bioch. 56: 547-550 (1992)   DOI
9 Hayashi T. The pectin enzyme produced by microorganisms. I. Pectin galacturonase from Aspergillus kawachii. J. Ferment. Technol. 36: 246-248 (1958)
10 Koseki T, Mese Y, Nishibori N, Masaki K, Fujii T, Handa T, Yamane Y, Shiono Y, Murayama T, Iefuji H. Characterization of an alpha-L-rhamnosidase from Aspergillus kawachii and its gene. Appl. Microbiol. Biot. 80: 1007-1013 (2008)   DOI   ScienceOn
11 Herber D, Phipps P, Strange P. Chemical analysis of microbial cells. Vol. 5B, pp. 210-344. In: Methods in Microbiology. Norris J, Ribbons D (eds). Academic Press, London, UK (1971)
12 Schols HA, Geraeds CCJM, Searle-van Leeuwen MF, Kormelink FJM, Voragen AGJ. Rhamnogalacturonase: A novel enzyme that degrades the hairy regions of pectins. Carbohyd. Res. 206: 105-115 (1990)   DOI   ScienceOn
13 Nagamine K, Murashima K, Kato T, Shimoi H, Ito K. Mode of $\alpha$-amylase production by the shochu koji mold Aspergillus kawachii. Biosci. Biotech. Bioch. 67: 2194-2202 (2003)   DOI   ScienceOn
14 Koseki T, Okuda M, Sudoh S, Kizaki Y, Iwano K, Aramaki I, Matsuzawa H. Role of two $\alpha$-L-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii, and Aspergillus awamori. J. Biosci. Bioeng. 96: 232-241 (2003)   PUBMED
15 Kitamoto K. Molecular biology of koji molds. Adv. Appl. Microbiol. 51: 129-146 (2002)   DOI   PUBMED
16 Yagi F, Fan J, Tadera K, Kobayashi A. Purification and characterization of carboxyl proteinase from Aspergillus kawachii. Agr. Biol. Chem. Tokyo 50: 1029-1033 (1986)   DOI
17 Klavons J, Bennett R. Determination of methanol using alcohol oxidase and its application to methyl ester content of pectins. J. Agr. Food. Chem. 34: 597-599 (1986)   DOI
18 Iwano K, Mikami S, Fukuda K, Shiinoki S, Shimada T. The properties of various enzymes of shochu koji (Aspergillus kawachii). J. Brew. Soc. Jpn. 81: 490-494 (1986)   DOI
19 Mikami S, Iwano K, Shinoki S, Shimada T. Purification and some properties of acid-stable $\alpha$-amylases from shochu koji (Aspergillus kawachii). Agr. Biol. Chem. Tokyo 51: 2495-2501 (1987)   DOI
20 Haard FN, Odunfa SA, Cherl-Ho L, Quinteros-Ramirez R, Lorence-Quinones A, Wacher-Radarte C. Fermented cereals. A global perspective. FAO Agricultural Services Bulletin No 138, Food and Agricultural Organization, Rome, Italy (1999)
21 Ride JP, Drysdale RB. A rapid method for the chemical estimation of filamentous fungi in plant tissue. Physiol. Plant Pathol. 2: 7-15 (1972)   DOI
22 Saha BC. $\alpha$-L-Arabinofuranosidases: Biochemistry, molecular biology, and application in biotechnology. Biotechnol. Adv. 18: 403-423 (2000)   DOI   PUBMED   ScienceOn
23 de Vries RP, Visser J. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microbiol. Mol. Biol. R. 65: 497-522 (2001)   DOI   ScienceOn