Streptomyces griseus Pronase” from

This group includes exopeptidases, carboxypep-tidases A and B, aminopeptidases, dipeptidases, prolidase and prolinase, and endopeptidases from bacteria and fungi, such as Bacillus cereus, B. megaterium, B. subtilits, B. ther-moproteolyticus (thermolysin), Streptomyces griseus (pronase it also contains carboxy- and aminopeptidases) and Aspergillus oryzae. 

Enzymatic gelation of partially heat-denatured whey proteins by trypsin, papain, pronase, pepsin, and a preparation of Streptomyces griseus has been studied (Sato et al., 1995). Only peptic hydrolysate did not form a gel. The strength of the gel depended on the enzyme used and increased with increasing DH. Hydrolysis of whey protein concentrate with a glutamic acid specific protease from Bacillus licheniformis at pH 8 and 8% protein concentration has been shown to produce plastein aggregates (Budtz and Nielsen, 1992). The viscosity of the solution increased dramatically during hydrolysis and reached a maximum at 6% DH. Incubation of sodium caseinate with pepsin or papain resulted in a 55-77% reduction in the apparent viscosity (Hooker et al., 1982). 

Sequence 1, in Table I, is the sequence of trypsin, chymotrypsin, pancreatic elastase, thrombin, and other mammalian proteases, and it occurs throughout the animal kingdom down to invertebrates as primitive as the sea anemone (4). The Streptomyces griseus enzymes are from Pronase, a commercial enzyme preparation. Two of its components, Streptomyces griseus trypsin and protease A, not only have the Asp.Ser.Gly sequence, but they show several other homologies in sequence with the mammalian enzymes (5, 6), The same is true for the sequence of a-lytic protease, the Myxobacter 495 enzyme (7). 

Pronase a mixture of at least 4 proteolytic enzymes from Streptomyces griseus. TWo peptide esterase components resembling chymotrypsin and trypsin have been separated and further characterized. Both are inhibited by chicken ovoinhibitor. 

In a previous study, we incubated chromatophores of Rps.caps. with a specific pronase (type III, Sigma) from Streptomyces griseus (5). The effect of pronase digestion on the spectral characteristics of both the field-sensitive and the field-insensitive carotenoid pools was monitored. It was shown that the field-responding carotenoids are more sensitive to pronase treatment than the non-responding pool. In the present study, these experiments were extended to other digestive treatments of chromatophores of Rhodopseudomonas capsulata as well as sphaeroides. 

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