PRODUCTION AND PURIFICATION OF AN ACTIVE BOVINE LYSOZYME IN TOBACCO (NICOTIANA-TABACUM) - UTILIZATION OF VALUE-ADDED CROP PLANTS TRADITIONALLY GROWN UNDER INTENSIVE AGRICULTURE

The goals of this study were to express bovine lysozyme in tobacco and to purify the protein with a scaleable process to >9O% homogeneity wh ile retaining antimicrobial characteristics. Results showed that the e nzyme was expressed at levels equivalent to 1-1.5% of total fraction 2 protein in each of five different transformant groups. The enzyme was subsequently purified to 93% homogeneity using an easily scaleable pr ocess while retaining high activity. It was concluded that tobacco was an excellent choice for expression of the recombinant protein and tha t the purification process developed in this study demonstrates method ology for isolation of high-value enzymes from tobacco and other crop plants.