Weitere Charakterisierung einer Chlorogensäure-Hydrolase aus Aspergillus niger / Further Characterization of a Chlorogenic Acid Hydrolase from Aspergillus niger
1980 ◽
Vol 35
(9-10)
◽
pp. 699-701
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Keyword(s):
Abstract In addition to our previous paper [1] further characteristics of the chlorogenic acid hydrolase are described. Polyacrylamid gelelectrophoresis revealed only one band for the purified enzyme. Sodium dodecyl-sulfate polyacrylamid gelelectrophoresis showed a molecular weight of 60000, demonstrating four subunits of the enzyme (total molecular weight 240000). The enzyme is stable in a pH-range of 3 .0 -8 .5 and up to a temperature of 55 °C. The temperature coefficient Q10 is 1.5, the activation energy EA is 6.0 kcal/mol. The amino acid analysis and substrate specificity data are given in tables. Essential for the enzyme activity is the C=C double bound neighbouring the ester linkage. The enzyme crystallizes in prisms.
2005 ◽
Vol 115
(1)
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pp. 47-56
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Keyword(s):
1974 ◽
Vol 31
(01)
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pp. 072-085
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2000 ◽
Vol 66
(1)
◽
pp. 252-256
◽
1998 ◽
Vol 64
(8)
◽
pp. 3029-3035
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Keyword(s):
1981 ◽
Vol 59
(4)
◽
pp. 256-261
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