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Portland Press, Biochemical Journal, 2(331), p. 513-519, 1998

DOI: 10.1042/bj3310513

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Purification and partial characterization of a peroxidase from plant cell cultures of Cassia didymobotrya and biotransformation studies.

Journal article published in 1998 by Alberto Vitali, Bruno Botta ORCID, G. Delle Monache, Giuliano Delle Monache, Sabrina Zappitelli, Paola Ricciardi, Sonia Melino, Raffaele Petruzzelli, Bruno Giardina
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

An acidic peroxidase (EC 1.11.1.7) produced by cell suspension cultures of Cassia didymobotrya (wild senna) was purified from culture medium collected on the 29th day. The enzyme was shown to be a glycoprotein with a pI of 3.5, a molecular mass of approx. 43 kDa by SDS/PAGE and 50 kDa by gel filtration. The N-terminal sequence was very similar to those of other plant peroxidases. The peroxidase was characterized by a high specificity towards coniferyl alcohol and other natural phenolics such as guaiacol and ferulic and caffeic acids. These findings suggest that the enzyme is involved in lignification processes of the cell wall. Moreover, the enzyme was able to catalyse the oxidation of 4,3',4'-trihydroxychalcone and 4, 3',4'-trihydroxy-3-methoxychalcone to the corresponding 3, 3'-biflavanones, as mixtures of racemic and meso forms.