49F-25 |
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R. BRIONES-MARTÍNEZ1, P. Cruz-Luna, G. Flores-Claros, M. I. Cortés-Vázquez, and B. Arroyo-Urióstegui. (1) Biotecnología/Laboratorio de Biofísica Molecular y Enzimología, Centro de Desarrollo de Productos Bióticos, Km 8 Carretera Yautepec-Jojutla, Yautepec, Morelos, 62731, Mexico Proteinases are enzymes with a wide range of applications in food and pharmaceutical industries. The juice obtained from the fruits of the mexican plant Bromelia hemisphaerica has been the source of a new polymorphic proteolytic enzyme with scientific and technological approaches: hemisphaericin. Recent studies were concerned with the plant pilot production of a refined preparation and the development of industrial applications; so, up to this moment still remain a problem to be solved: a formula with additives that can provide a long term storage stability without a great loss of enzyme activity. The objective in this study was to determine the effect of soluble additives on enzyme activity stability of refined hemisphaericin liquid preparations Caseinolytic residual activity was measured in hemisphaericin mixtures with soluble additives (glycerol 20%, polyethyelene glycol 20%; propylene glycol 20%; sodium metabisulphite 2.5%; glycerol 10% + sodium metabisulphite 1%) stored at 5 °C. The additives which showed better results in maintaining high levels of residual proteolytic activity (near to 100%) for refined hemisphaericin after a period of five months of storage, were sodium metabisulphite, followed by glycerol-sodium metabisulphite. The present results, in spite of being preliminary, allowed the generation of a data base useful to design a strategy for stabilization of liquid hemisphaericin preparations with large shelf stability.
Session 49F, Fruit & Vegetable Products: Fresh vegetables
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