Bromelain composition

Y. Yasuda, N. Takahashi, and T. MundiL Hie composition and structure of casho-hydrate moiety of stem bromelain. Biochemistry 9 25 (1970). 

Part Three reviews representative multienzyme compositions, such as pancxeatin, as well as premising recent developments with glucocerebtosidaae, deoxyribonuclease and protein inhibitors of elastase. This part integrates biochemical, experimental, and clinical data of therapeutic enzymes, such as asparaginase, bromelain, hyaluronidase, and cysteine proteinsses, about which... 

For historical reasons many pharmaceutical enzymes are assayed with physiological or biopolymeric substrates (proteins, polysaccharides, bacteria, oil emulsions), which causes a number of theoretical and practical problems. The interpretation of results is difficult when natural substrates are converted into products that are substrates themselves for the next enzymatic attack. Reaction rates often depend on the position of the scissile bonds in the molecule and the chemical nature of the moieties. Hydrolysis can proceed simultaneously on various bonds at various rates. In proteolysis it is assumed that some products are liberated only after denaturation and that during the reaction course new peptide bonds become accessible for hydrolysis. In these cases the enzymatic mechanisms become exceedingly complex, kinetic parameters are apparent values, and experimental results are strongly influenced by the reaction conditions. Reproducibility problems can occur upon assaying proteinases with a limited specificity for particular casein types. Bromelain and pancreatic proteinase, FEP pharmaceutical enzyme standards, are assayed with a casein substrate. The extent of soluble peptide release is a measure of proteolytic activity. However, due to limited specificity, some proteinases release peptides with a nonrandom aromatic amino acid composition. Contamination of casein preparations with protein and of test enzyme substances with other proteinases biases the assay results. Under these conditions, relative assay methods are indicated. 

Williams reported the enzymatic hydrolysis of poly(L-lactic acid) (PLLA) in the presence of enzymes such as pronase, proteinase K, and bromelain. However, these enzymes are proteases and not PLLA depolymerases [3]. Regarding PLA stereocopolymers, Fukuzaki et al. reported that the hydrolysis of PLA was accelerated in the presence of specific enzymes and the most rapid enzymatic degradation of the stereocopolymers was observed on the poly(DL-lactic acid) (PDLLA) sample containing 50% L-lactic acid (LLA) [4]. Furthermore, Makino et al. showed that the addition of a carboxylic esterase accelerated a decrease in the weight-average molecular weight of PDLLA [5]. Reeve et al. reported the effects of stereochemical composition on enzymatic degradability of PLA films by proteinase K from Tritirachium album [6]. 

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