Characteristics and applcation of immobilized papain in a continuous flow reactor

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R Chiou; LR Beuchat

Type of Document:
Scholarly Article


Biotechnology and Applied Biochemistry

Date of Publication:

Place of Publication:
Not Available


Abstract: Papain was immobilized on an anion-exchange resin by physical adsorption followed by cross-linking with glutaraldehyde. The activity and rate of heat inactivation of the enzyme was determined at 37 to 95 degrees C. Activity increased with an increase in temperature up to 85 degrees C, then decreased slightly at 95 degrees C. Activation of the enzyme by cysteine in 2 mM EDTA increased proportionally with an increase in concentration from 0.004 to 0.12 M. Levels of dissolved oxygen in solutions of EDTA containing cysteine in a closed system and with nitrogen purging in the absence of cysteine in an open system were monitored at 51 degrees C. Both the presence of cysteine and purging with nitrogen were effective in depleting dissolved oxygen. The final oxygen level was essentially independent of cysteine concentrations of 0.01, 0.02, and 0.10 M, and was reached in 95, 85, and 55 min, respectively. However, final levels of oxygen were dependent upon the flow rate of nitrogen from 1 to 10 SLPM and were reached within 15 min. Immobilized papain in a continuous-flow stirred-tank (300 rpm) reactor with a 4-liter reaction volume accompanied by nitrogen purging of 4 SPLM was used to hydrolyze a 1.5% casein solution in the presence of 0.01 M cysteine in 2 mM EDTA at 51 degrees C. The reaction rate was 1 liter/h and activity was measured based on the Content of trichloroacetic acid-soluble protein in the outflow. Papain activity was not observed to decrease during a 30-h reaction period

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