Two forms (A and B) of Bromelain with similar specificity have been isolated from pineapple stem (1). Bromelain hydrolyzes proteins, peptides, amides and esters of amino acids and peptides; preferential cleavage site is the carbonyl end of lysine, alanine, tyrosine and glycine (1,2). For relative activities on a number of amino acid substrates see Barman (3). The following side activities can be detected in Bromelain preparations: amylase, phosphatase, peroxidase, the latter being very labile upon storage.