SCREENING OF HIGHER PLANTS PROTEASES AS CATALYST FOR THE SYNTHESIS OF ARGININE- BASED CATIONIC SURFACTANTS

MORCELLE, S.; N. PRIOLO; N. O. CAFFINI; D. OBREGÓN; C. LIGGIERI; C. E. SALAS; M. T. LOPES; M. T. GOMES; M. C. MORÁN; J. CASTILLO; M. R. INFANTE; P. CLAPES

Barcelona, España

Conferencia; 6th Green Chemistry Conference; 2004

Organizado por el Institut Univ. de Ciència i Tecnologia (IUCT)

Lipoamino acids constitute an interesting class of low-toxicity environmentally friendly surfactants with excellent emulsifying properties and strong antimicrobial activity.They can be regarded as an alternative to conventional synthetic surfactants in which the three fundamental requirements for industrial development are present: (a) low toxicity, (b) multifunctionality, and (c) renewable sources of raw materials. These characteristics make them candidates of choice as additives in pharmaceutical, food and cosmetic formulations. The interest for amino acid-based surfactants lies also in their synthesis, which can be achieved by biotechnological methods. In this concern, developments in enzyme technology have opened new possibilities for the synthesis of surfactants from natural sources. Proteolytic enzymes of plant origin have received special attention due to their high degree of proteolytic activity with an abundant and cheap availability. In this concern, there is a need for discovering new plant sources of potent, more active and more specific proteolytic enzymes. Our interest in amino acid-based surfactants and in biotechnology has led us to study the enzymatic synthesis of N-alkyl amide derivatives of arginine. The study is focused on two aspects. First, the characterization of the proteolytic properties of crude extracts from the latex of three species belonging to the Asclepiadaceae family (Araujia angustifolia, Araujia hortorum and Funastrum clausum) and one belonging to the Caricaceae family (Carica candamarcensis) is reported. The proteases present in the crude extracts showed the main characteristics of the cysteine proteolytic class (optimum pH, optimum temperature, isoelectric point, stability). Secondly, the papain-like proteolytic activity of the four crude extracts were proved and compared with commercial papain for the synthesis of arginine-based cationic surfactants.