Proteolytic activity of Oidiodendron kalrai

1975 ◽  
Vol 21 (9) ◽  
pp. 1362-1368 ◽  
Author(s):  
P. M. Cino ◽  
R. P. Tewari
Keyword(s):  
Basement Membrane ◽  
Enzymatic Activity ◽  
Human Serum ◽  
Proteolytic Activity ◽  
Crude Extract ◽  
Protease Activity ◽  
Proteolytic Enzymes ◽  
Cell Free Extract ◽  
Yeast Phase ◽  
Biological Substrates

The physiochemical characteristics of the intracellular proteolytic enzymes of Oidiodendron kalrai, a neuropathogenic fungus, were studied. The organism in the yeast phase was grown in a semisynthetic medium containing 1% tryptone, at 37 °C for 48 h, on a gyrotory shaker. The crude extract was prepared by breaking the cells in a French pressure cell and the proteolytic activity was tested against biological substrates. The cell-free extract hydrolyzed casein, hemoglobin, lactalbumin, gelatin, elastin, collagen, and purified rabbit renal basement membrane to various degrees. Optimal proteolytic activity was observed at pH 6 and at 32 °C. Calcium and EDTA did not affect the enzymatic activity; however, activity was partially inhibited by sulfhydryl-blocking agents and by heat-inactivated horse, calf, and human serum. The extract was totally inactivated by exposure to a temperature of 70 °C for 60 min. Storage at −76 °C or −15 °C for 6 months or at 4 °C for 4 weeks did not affect protease activity.

Purification of Oidiodendron kalrai proteases

1976 ◽  
Vol 22 (3) ◽  
pp. 327-333 ◽  
Author(s):  
P. M. Cino ◽  
R. P. Tewari
Keyword(s):  
Ammonium Sulfate ◽  
Proteolytic Activity ◽  
Column Chromatography ◽  
Crude Extract ◽  
Proteolytic Enzymes ◽  
Deae Cellulose ◽  
Ammonium Sulfate Precipitation ◽  
Proteolytic Activities ◽  
Yeast Phase ◽  
Cellulose Column

Oidiodendron kalrai yeast-phase cells demonstrate proteolytic activity. Some of the proteolytic enzymes of the crude extract were purified by a combination of ammonium sulfate precipitation, Sephadex G-200, and diethylaminoethyl (DEAE) cellulose column chromatography. At least six proteins exhibiting a range of proteolytic activities could be identified by these procedures. Purity of the enzyme fractions obtained from the DEAE-cellulose columns was tested by running polyacrylamide gels.

scholarly journals Aktivitas Enzimatis Isolat Bakteri Asam Laktat dari Saluran Pencernaan Kepiting Bakau (Scylla spp.) Sebagai Kandidat Probiotik [Activity Enzymatic of Isolate Lactic Acid Bacteria from the Digestive Tract of Mud Crab (Scylla spp.) as a Candidate Probiotics]

2019 ◽  
Vol 8 (2) ◽  
pp. 94
Author(s):  
Pipin Suciati ◽  
Wahju Tjahjaningsih ◽  
Endang Dewi Masithah ◽  
Heru Pramono
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Enzymatic Activity ◽  
Digestive Tract ◽  
Proteolytic Activity ◽  
Biochemical Characterization ◽  
Proteolytic Enzymes ◽  
Lipolytic Activity ◽  
Mud Crab ◽  
Mangrove Crab

Abstrak Probiotik dapat didefinisikan sebagai mikroba hidup yang ditambahkan dalam jumlah tertentu yang mampu bertahan hidup dalam ekosistem saluran pencernaan. Enzim yang dihasilkan oleh mikroba yang diisolasi dari saluran pencernaan ikan dapat digunakan sebagai probiotik. Enzim proteolitik ekstraseluler secara alami diproduksi oleh mikroba untuk menghidrolisis polipeptida dalam media menjadi peptida dan asam amino. Bakteri asam laktat dapat menghasil enzim seperti protease, α-amilase, fitase, kitinase, lipase. Penelitian ini bertujuan untuk mendapatkan isolat bakteri asam laktat dari saluran pencernaan kepiting bakau (Scylla spp.) yang mempunyai aktivitas proteolitik. Penelitian ini menggunakan metode deskriptif berupa aktivitas enzimatis dan karakterisasi uji biokimia isolat bakteri asam laktat dari saluran pencernaan kepiting bakau (Scylla spp.). Jumlah kepiting bakau yang digunakan adalah 10 ekor. Hasil penelitian didapatkan tiga isolat bakteri asam laktat yang memiliki aktivitas proteolitik kuat, yaitu WK 28, WK 33, dan WK 53. Hasil uji biokimia isolat WK 28 termasuk ke dalam genus Pediococcus sp., isolat WK 33 termasuk ke dalam Lactobacillus sp., dan isolat WK 53 termasuk ke dalam genus Streptococcus sp. WK 28 (Pediococcus sp.) dan WK 33 (Lactobacillus sp.) mempunyai aktivitas proteolitik dan aktivitas lipolitik. Isolat WK 53 (Streptococcus sp.) mempunyai aktivitas enzimatis yaitu aktivitas proteolitik, amilolitik, dan lipolitik. Abstract Probiotics are defined as live microbes are added in a certain amount that is able to survive in the digestive tract ecosystem. Enzymes produced by microbes isolated from the digestive tract of fish can be used as probiotics. Extracellular proteolytic enzymes naturally produced by the microbes to hydrolyze a polypeptide in a media into peptides and amino acids. Lactic acid bacteria can produce enzymes such as proteases, α-amylase, phytase, chitinase, lipase. This study aims to get the lactic acid bacteria isolates from the gastrointestinal tract of mangrove crab (Scylla spp.) That have proteolytic activity. This research uses descriptive method such as enzymatic activity and biochemical characterization of isolates of lactic acid bacteria from the digestive tract of mangrove crab (Scylla spp.). Amount of mud crab used is 10 fish. The result showed three isolates of lactic acid bacteria that have a strong proteolytic activity, namely WK 28 WK 33 and WK 53. The results of biochemical tests WK 28 isolates belonging to the genus Pediococcus sp., Isolate WK 33 belonging to the Lactobacillus sp., And WK 53 isolates belonging to the genus Streptococcus sp. WK 28 (Pediococcus sp.) And WK 33 (Lactobacillus sp.) Have proteolytic activity and lipolytic activity. Isolates WK 53 (Streptococcus sp.) Have enzymatic activity is proteolytic activity, amylolytic, and lipolytic.

scholarly journals Effect of Plant Growth Regulators on Protease Activity in Forest Floor of Norway Spruce Stand

Forests ◽  
2021 ◽  
Vol 12 (6) ◽  
pp. 665
Author(s):  
Ladislav Holik ◽  
Jiří Volánek ◽  
Valerie Vranová
Keyword(s):  
Organic Matter ◽  
Proteolytic Activity ◽  
Protease Activity ◽  
Forest Floor ◽  
Soil Microbial Activity ◽  
Inhibitory Effects ◽  
Chlorocholine Chloride ◽  
Soil Microbial ◽  
Native Soil ◽  
Transformation Processes

Soil proteases are involved in organic matter transformation processes and, thus, influence ecosystem nutrient turnovers. Phytohormones, similarly to proteases, are synthesized and secreted into soil by fungi and microorganisms, and regulate plant rhizosphere activity. The aim of this study was to determine the effect of auxins, cytokinins, ethephon, and chlorocholine chloride on spruce forest floor protease activity. It was concluded that the presence of auxins stimulated native proteolytic activity, specifically synthetic auxin 2-naphthoxyacetic acid (16% increase at added quantity of 5 μg) and naturally occurring indole-3-acetic acid (18%, 5 μg). On the contrary, cytokinins, ethephon and chlorocholine chloride inhibited native soil protease activity, where ethephon (36% decrease at 50 μg) and chlorocholine chloride (34%, 100 μg) showed the highest inhibitory effects. It was concluded that negative phytohormonal effects on native proteolytic activity may slow down organic matter decomposition rates and hence complicate plant nutrition. The study enhances the understanding of rhizosphere exudate effects on soil microbial activity and soil nitrogen cycle.

Ionophoric polyphenols are permeable to the blood–brain barrier, interact with human serum albumin and Calf Thymus DNA, and inhibit AChE enzymatic activity

2020 ◽  
Vol 29 (11) ◽  
pp. 1956-1975
Author(s):  
Alberto Martínez ◽  
Mai Zahran ◽  
Miguel Gomez ◽  
Johnny Guevara ◽  
Rosemary Pichardo-Bueno ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Enzymatic Activity ◽  
Human Serum ◽  
Blood Brain Barrier ◽  
Brain Barrier ◽  
Calf Thymus Dna ◽  
Blood Brain ◽  
Calf Thymus

scholarly journals FURTHER STUDIES ON THE ROLE OF PROTEASES IN THE ALLERGIC REACTION

1961 ◽  
Vol 113 (2) ◽  
pp. 359-380 ◽  
Author(s):  
Georges Ungar ◽  
Takuso Yamura ◽  
Jacqueline B. Isola ◽  
Sidney Kobrin
Keyword(s):  
Amino Acid ◽  
Guinea Pig ◽  
Proteolytic Activity ◽  
Guinea Pigs ◽  
Protease Activity ◽  
Amino Acid Esters ◽  
Protein Substrates ◽  
Protease Activation ◽  
Acid Esters

Protease activity was measured through the hydrolysis of synthetic amino acid esters in body fluids and tissues of guinea pigs, rats, mice, and humans. Significant in vitro activation was observed in serum and lung slices of sensitized guinea pigs on addition of the specific antigen. Increased proteolytic activity was also seen in reverse anaphylaxis. More marked activation occurred when guinea pig serum was treated with peptone and guinea pig or rat serum was treated with agar. Protease activation was demonstrated in specimens of human skin under the influence of a poison ivy extract or croton oil added in vitro. Urinary protease activity of guinea pigs increased significantly during the first hours of anaphylactic shock and very markedly in peptone shock. Peptone shock, elicited in mice pretreated with H. pertussis, was accompanied by a considerable increase in protease activity in the peritoneal fluid as compared with non-pretreated mice which were insensitive to peptone. Proteolytic activity resulting from the activation procedures was due to a number of proteases. The dominant substrate affinity and inhibition patterns suggest that serum and urine proteases are similar to but not identical with plasmin. Anaphylactic activation exhibited patterns different from those resulting from the action of anaphylactoid agents. Tissue enzymes are either of cathepsin- or chymotrypsin-type or mixtures of both. Some of the activated enzymes, although remarkably effective in hydrolyzing amino acid esters, show no activity on protein substrates. This does not justify, however, their designation as "esterases." They probably belong to the class of specific proteases acting only on a single or a small number of functionally significant protein substrates. There is at present sufficient evidence to prove not only that protease activation does occur in anaphylaxis and anaphylactoid conditions but also that it is an important component of the chain of reactions leading to the allergic response.

Influence of Neurosecretory Cells and of Corpus Allatum on Intestinal Protease Activity in the Adult Calliphora Erythrocephala MEIG

1963 ◽  
Vol 40 (2) ◽  
pp. 301-321
Author(s):  
ELLEN THOMSEN ◽  
IB MØLLER
Keyword(s):  
Protein Synthesis ◽  
Protease Activity ◽  
Proteolytic Enzymes ◽  
Specific Protein ◽  
Neurosecretory Cells ◽  
Corpus Allatum ◽  
Minor Effect ◽  
Calliphora Erythrocephala ◽  
Sugar Water ◽  
The Mean

1. The protease activity of the adult Calliphora female measured on the first 5 days after emergence was found to be highly influenced by the diet, the activity of females fed on sugar, water and meat (meat-flies) being much higher than that of females fed only on sugar and water (sugar-flies). 2. The development of the enzyme(s) was found to be controlled by the medial neurosecretory cells (m.n.c.), the mean protease activity of females deprived of their m.n.c. only amounting to one-quarter to one-third of the maximum values for the meat-flies. 3. Implantation of corpora cardiaca-allata (presumably containing m.n.c. hormone) into females without m.n.c. raised the protease activity of these significantly, showing that the influence of the implanted organs must be hormonal. 4. The corpus allatum was found to have a certain, if minor, effect on the protease activity. 5. It is concluded that in Calliphora the eating of meat exerts its effect on the production of protease mainly indirectly by causing liberation of m.n.c. hormone into the blood. 6. As proteases are themselves proteins, the effect of the m.n.c. hormone on the production of proteolytic enzymes by the gut cells must be regarded as an effect on the specific protein synthesis of these cells. There is some evidence that the m.n.c. hormone might be involved in the regulation of protein synthesis in general.

Resistance of Phlebotomus papatasi to infection with Leishmania donovani is modulated by components of the infective bloodmeal

Parasitology ◽  
1998 ◽  
Vol 117 (5) ◽  
pp. 467-473 ◽  
Author(s):  
Y. SCHLEIN ◽  
R. L. JACOBSON
Keyword(s):  
Proteolytic Activity ◽  
Trypsin Inhibitor ◽  
Alkaline Protease ◽  
Protease Activity ◽  
Leishmania Donovani ◽  
Blood Feeding ◽  
Growth Conditions ◽  
Enzymatic Activities ◽  
Phlebotomus Papatasi ◽  
Proteolytic Activities

The circumstances which permit the establishment of Leishmania infections in sandflies were investigated by altering the growth conditions for L. donovani parasites in the unsuitable vector Phlebotomus papatasi. Only 5·0% of the sandflies harboured a few parasites 3 days after feeding on promastigotes in defibrinated blood. Heparinized blood or the addition of trypsin inhibitor to the meals allowed persistence of infections (day 6) in 9·9% and 25·8% of the flies respectively. Meals of erythrocytes, saline and amastigotes produced 44·4% fly infection on day 6, while similar promastigote-initiated infections remained in 70·3% of the flies. Proteolytic activities in the guts of sandflies fed on the above meals without parasites, were the highest after defibrinated bloodmeals. Erythrocytes with saline decreased the maximal alkaline protease level from 20·8 U to 13·5 U/fly; that of trypsin from 3·9 U to 1·8 U/fly and that of the aminopeptidase from 5·5 U to 3·9 U/fly. After meals of heparinized blood, the maximal alkaline protease activity (12·0 U/fly) was also much lower than after defibrinated blood-feeding. The different diets which resulted in comparatively low enzymatic activities, including blood with trypsin inhibitor, also promoted the survival of infections. This implies that the proteolytic activity in the sandfly gut modulates the vector susceptibility.

scholarly journals Proteolytische Aktivität der lysosomalen Enzyme in der Leber wachsender Mäuse

2000 ◽  
Vol 43 (4) ◽  
pp. 363-374
Author(s):  
M. Schmidt ◽  
T. Król ◽  
U. Renne ◽  
L. Panicke
Keyword(s):  
Postnatal Development ◽  
Proteolytic Activity ◽  
Cathepsin D ◽  
Proteolytic Enzymes ◽  
Body Growth ◽  
Male Mice ◽  
High Body

Abstract. Title of the paper: Lysosomal proteolytic activity in the liver of growing mice The behaviour of the activity of some lysosomal proteolytic enzymes in Üie liver of mice, both selected and unselected for high body growth, was followed during the postnatal development. The activity of cathepsin D and L, the alanylaminopeptidase, the arginylaminopeptidase, the α-glucosidase and the N-acetyl-glucosaminidase was estimated in male mice aging 21, 28, 35 and 42 days. In the liver of animals with high body gain statistic significant lower activities (30–50 %) of all estimated enzymes were found, in comparison to the control mice. These results confirm the Statement mat inhibition of proteolysis is an immediate mechanism in the induction of growth.

scholarly journals SELECTED PROTEOLYTIC ACTIVITY BY EXTRACTS OF DERMESTID LARVAE

2011 ◽  
Vol 19 (19) ◽  
pp. 79-83
Author(s):  
Lavinel G. IONESCU
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Proteolytic Activity ◽  
Specific Activity ◽  
Proteolytic Enzymes ◽  
High Specific Activity ◽  
Water Extract ◽  
Dermestes Maculatus ◽  
Crude Preparation

The larvae of the Beetle Dermestes maculatus De Geer can subsist on a diet consisting largely of protein. Studies have been undertaken to investigate the nature of proteolytic enzymes. A water extract of the larvae yielded a crude preparation that hydrolyzes gelatin, bide powder, hemoglobin substrate, benzoyl-DL-arginine p-nitroamilide, and glutaryl-L-phenylalanine p-nitroanilide. Enzyme activity was found in a non-dialyzable, heat- and acid0labile portion of the extract yielded two fractions with high specific activity towards gelatin. These are precipitated between 40% to 60% saturation of ammonium sulfate and 60% to 80% saturation. The higher specific activity was observed in the 40%-60% fraction. These results suggest that the larvae of these dermestids contain proteolytic enzymes with actions similar to mammalian trypsin and chymotrypsin. The results also suggest that other proteolytic enzymes may be present as well.

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