Polygalacturonase Activity in Yellow Pitaya Peel (Acanthocereus pitajaya)

Polygalacturonase activity was determinated in yellow pitaya fruit (Acanthocereus pitajaya). Protein concentrations and activities of the enzyme in the extracts weredetermined. Buffer sodium phosphate 20 mM pH 7,0 with NaCl 0,5 M was the most effective extraction system. The enzyme exhibited optimum activity at pH 5,0 in buffer citrate at 40 °C. The KM of the enzyme was 2.9 mg/mL for polygalacturonic acid and VMÁX of 0.076 nmol of reducing groups/s. Results show that polygalacturonase is related with softening on yellow pitaya fruit.

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Bibliographic Details
Main Authors: Rodríguez Castro, Johanna Paola, Narváez Cuenca, Carlos Eduardo, Restrepo Sánchez, Luz Patricia
Format: Digital revista
Language:spa
Published: Universidad Nacional de Colombia - Sede Bogotá - Facultad de Ciencias - Departamento de Biología 2006
Online Access:https://revistas.unal.edu.co/index.php/actabiol/article/view/27157
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Summary:Polygalacturonase activity was determinated in yellow pitaya fruit (Acanthocereus pitajaya). Protein concentrations and activities of the enzyme in the extracts weredetermined. Buffer sodium phosphate 20 mM pH 7,0 with NaCl 0,5 M was the most effective extraction system. The enzyme exhibited optimum activity at pH 5,0 in buffer citrate at 40 °C. The KM of the enzyme was 2.9 mg/mL for polygalacturonic acid and VMÁX of 0.076 nmol of reducing groups/s. Results show that polygalacturonase is related with softening on yellow pitaya fruit.