Reduction of disulfide bonds by Streptomyces pactum during growth on chicken feathers
Article Abstract:
Streptomyces pactum causes the disintegration of chicken feathers in the presence of keratinolytic proteinases and extracellular reduction of disulfide bonds. The use of oxidized glutathione as a substrate provides the conditions necessary for disulfide reduction. The reduction of glutathione depends on the presence of metabolically active cells. The reaction fails to show evidence for long-term direct contact between mycelium and substrate for keratin degradation. The mycelium also reduces tetrazolium dyes and cystine.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530
Article Abstract:
A proteinase produced by and isolated from Streptomyces pactum DSM 40530 may be more effective than previously available enzymes for partially breaking down keratin. The enzyme broke down insoluble substances such as keratin azure, feather meal, and chicken feather downs. However, in order for the enzyme to make a large percentage of the keratin soluble, it had to be used along with dithiothreitol. The specificity and optimum termperature and pH conditions for enzyme activity are discussed.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1995
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The effects of adding lactococcal proteinase on the growth rate of Lactococcus lactis in milk depend on the type of enzyme
Article Abstract:
Raising the proteolytic activity of Lactococcus lactis cultures in milk by including the corresponding proteinase improved the growth rate in spite of the strain and the type of proteinase. This indicated that the rate of casein degradation is a main factor in the growth rate limitation of L. lactis in milk. However, the stimulation was only temporary and the decrease in the growth rate in the poststimulation phase was dependent on the kind of cell envelope proteinase.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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