The structural chemistry of the Bacillus thuringiensis parasporal protein crystal is discussed in terms of purification techniques, removal of contaminating proteases, crystal subunit size, crystal shape, interchain crosslinks, the ultimate toxin, and lysinoalanine. The alkaline pH cleavage of disulfide bonds is stressed in relationship to this role in crystal solubilization and toxin formation. The future implication s of plasmid‐coded crystal formation and B. thuringiensis var. israelensis (effective against mosquitoes and black flies) are also discussed.
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology