RELEASE OF INTRACELLULAR β-GALACTOSIDASE FROM LACTOBACILLUS ACIDOPHILUS AND L-ASPARAGINASE FROM PECTOBACTERIUM CAROTOVORUM BY HIGH-PRESSURE HOMOGENIZATION

Abstract

This article reports a comparison of the ease of disruption of gram-positive (Lactobacillus acidophilus) and gram-negative (Pectobacterium carotovorum) bacteria using high-pressure homogenization (HPH). The location factor for both enzymes calculated from enzyme release kinetics together with localization studies identified them as cytoplasmic enzymes. The results showed that release of β-galactosidase by HPH of L. acidophilus was more difficult than the release of L-asparaginase from P. carotovorum. It took nine passes at 55.14 MPa for maximum release of β-galactosidase (0.949 IU/mL) as compared to six passes at 41.35 MPa for L-asparaginase (4.653 IU/mL); 1.7 IU of β-galactosidase was released as against 11.5 IU of L-asparaginase per MJ of energy during high-pressure homogenization.

Keywords:

• β-galactosidase
• Enzyme localization
• High-pressure homogenization (HPH)
• L-asparaginase
• Location factor

Acknowledgments

The authors would like to acknowledge Technical Education Quality Improvement Programme (TEQIP) and University Grants Commission (UGC) for financial support for this project.