Isolation and Properties of Stachyrase A, a Chymotrypsin-Like Serine Proteinase from Stachybotrys chartarum

ABSTRACT A strain of the common mold Stachybotrys chartarum has been isolated from the lung of a child with pulmonary hemorrhage. We report the purification of stachyrase A, a new serine chymotrypsin-like proteinase from S. chartarum. This enzyme cleaves major protease inhibitors, several biologically active peptides, and collagen, all of which are found in the lung.

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Application of Asian pumpkin (Cucurbita ficifolia) serine proteinase for production of biologically active peptides from casein.

Acta Biochimica Polonica ◽

10.18388/abp.2013_1960 ◽

2013 ◽

Vol 60 (1) ◽

Cited By ~ 6

Author(s):

Anna Dąbrowska ◽

Marek Szołtysik ◽

Konrad Babij ◽

Marta Pokora ◽

Aleksandra Zambrowicz ◽

...

Keyword(s):

Antimicrobial Activity ◽

Free Amino ◽

Serine Proteinase ◽

Biologically Active ◽

Amino Group ◽

Active Peptides ◽

Rp Hplc ◽

Amino Group Content ◽

Biologically Active Peptides ◽

Peptide Profiles

The main objective of this study was to determine potential application of a serine proteinase derived from Asian pumpkin for obtaining biologically active peptides from casein. The course of casein hydrolysis by three doses of the enzyme (50, 150, 300 U/mg of protein) was monitored for 24 hours by the determinations of: hydrolysis degree DH (%), free amino group content (μmole Gly/g), RP HPLC peptide profiles and by polyacrylamide gel electrophoresis. In all hydrolyzates analyzed antioxidant activities were determined using three tests: the ability to reduce iron ions in FRAP test, the ability to scavenge free radicals in DPPH test, and Fe(2+) chelating activity. The antimicrobial activity of obtained peptide fractions was determined as the ability to inhibit the growth of Escherichia coli, Bacillus cereus and Pseudomonas fluorescens in a diffusion plate test. The deepest degradation, expressed as the DH [%] and the free amino group content (67% and 7528 µmole Gly/mg, respectively), was noted in samples hydrolyzed with 300 U/ml of enzyme for 24 hours, while in other samples the determined values were about three and two times lower. The results were in agreement with the peptide profiles obtained by RP HPLC. The highest antioxidative activities determined in all tests were seen for the casein hydrolysate obtained with 300 U/mg protein of serine proteinase after 24 h of reaction (2.15 µM Trolox/mg, 96.15 µg Fe(3+)/mg, 814.97 µg Fe(2+)/mg). Antimicrobial activity was presented in three preparations. In other samples no antimicrobial activity was detected.

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CONTROL OF INTESTINAL ABSORPTION OF BIOLOGICALLY ACTIVE PEPTIDES BY VARIOUS PROTEASE INHIBITORS

Drug Metabolism and Pharmacokinetics ◽

10.2133/dmpk.9.supplement_94 ◽

1994 ◽

Vol 9 (supplement) ◽

pp. 94-97

Author(s):

Akira YAMAMOTO ◽

Toshio TANIGUCHI ◽

Takuya FUJITA ◽

Masahiro MURAKAMI ◽

Shozo MURANISHI

Keyword(s):

Intestinal Absorption ◽

Protease Inhibitors ◽

Biologically Active ◽

Active Peptides ◽

Biologically Active Peptides

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The phylogeny of the common peptides (Chairman’s address)

Proceedings of the Royal Society of London Series B Biological Sciences ◽

10.1098/rspb.1980.0118 ◽

1980 ◽

Vol 210 (1178) ◽

pp. 61-62 ◽

Cited By ~ 6

Keyword(s):

Cellular Localization ◽

Neuroendocrine System ◽

Biologically Active ◽

The Other ◽

Active Peptides ◽

Diffuse Neuroendocrine System ◽

Biologically Active Peptides ◽

Neuroactive Peptides ◽

The Common ◽

The One

The cellular localization of peptides, the detection of peptidergic pathways and the regulation and release of putative neurotransmitters, the three subjects dealt with in this session, are all of paramount interest and importance. They hardly require a Chairman’s address, however, and since there is no time for what Professor Schwyzer calls a sychnology, I offer instead a brachylogy on the phylogeny of the common peptides, the common neuroactive peptides, that is. The common peptides are those 20 or so biologically active peptides found, on the one hand, in the cells and processes of the central and peripheral divisions of the nervous system and, on the other, in the cells and processes of the central and peripheral divisions of the diffuse neuroendocrine system. In brief, they are common to brain and gut.

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