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Tytuł:
Evaluation of P1 substrate specificity of staphylococcal SplB protease
Autorzy:
Pustelny, Katarzyna
Stach, Natalia
Wladyka, Benedykt
Dubin, Adam
Dubin, Grzegorz
Powiązania:
https://bibliotekanauki.pl/articles/1039355.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
serine protease
serine protease-like
SplB
Staphylococcus aureus
substrate specificity
Opis:
Staphylococcus aureus is a dangerous human pathogen characterized by growing antibiotic resistance. Virulence of S. aureus relies on a variety of secreted and cell surface associated virulence factors among which certain proteolytic enzymes play an important role. Amid staphylococcal extracellular proteases, those encoded by the spl operon remain poorly characterized, both in terms of enzymology and their physiological role. Initial data demonstrated that Spl proteases exhibit restricted substrate specificity. This study describes development of convenient protein FRET substrates for SplB protease and characterization of the substrate preference of the protease at the P1' position. Kinetic data on hydrolysis of a panel of substrates substituted at the said position is provided.
Źródło:
Acta Biochimica Polonica; 2014, 61, 1; 149-152
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
In silico studies of selected xanthophylls as potential candidates against SARS-CoV-2 targeting main protease (Mpro) and papain-like protease (PLpro)
Autorzy:
Karpiński, T.M.
Kwaśniewski, M.
Ożarowski, M.
Alam, R.
Powiązania:
https://bibliotekanauki.pl/articles/2049355.pdf
Data publikacji:
2021
Wydawca:
Instytut Włókien Naturalnych i Roślin Zielarskich
Tematy:
protease
papain-like protease
xanthophyll
coronavirus
COVID-19
antiviral activity
koronawirus
pandemia
działanie przeciwwirusowe
projektowanie leków wspomagane komputerowo
Opis:
Introduction: The main protease (Mpro) and the papain-like protease (PLpro) are essential for the replication of SARS-CoV-2. Both proteases can be targets for drugs acting against SARS-CoV-2. Objective: This paper aims to investigate the in silico activity of nine xanthophylls as inhibitors of Mpro and PLpro. Methods: The structures of Mpro (PDB-ID: 6LU7) and PLpro (PDB-ID: 6W9C) were obtained from RCSB Protein Data Bank and developed with BIOVIA Discovery Studio. Active sites of proteins were performed using CASTp. For docking the PyRx was used. Pharmacokinetic parameters of ADMET were evaluated using SwissADME and pkCSM. Results: β-cryptoxanthin exhibited the highest binding energy: –7.4 kcal/mol in the active site of Mpro. In PLpro active site, the highest binding energy had canthaxanthin of –9.4 kcal/mol, astaxanthin –9.3 kcal/mol, flavoxanthin –9.2 kcal/mol and violaxanthin –9.2 kcal/mol. ADMET studies presented lower toxicity of xanthophylls in comparison to ritonavir and ivermectin. Conclusion: Our findings suggest that xanthophylls can be used as potential inhibitors against SARS-CoV-2 main protease and papain-like protease.
Źródło:
Herba Polonica; 2021, 67, 2; 1-8
0018-0599
Pojawia się w:
Herba Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel alkaline protease from wild edible mushroom Termitomyces albuminosus
Autorzy:
Zheng, Suyue
Wang, Hexiang
Zhang, Guoqing
Powiązania:
https://bibliotekanauki.pl/articles/1039935.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
alkaline protease
mushroom
Termitomyces albuminosus
purification
Opis:
A protease with a molecular mass of 30 kDa and the N-terminal sequence of GLQTNAPWGLARSS, was isolated from fresh fruiting bodies of the wild edible mushroom Termitomyces albuminosus. The purification protocol included ion exchange chromatography on DEAE-cellulose, Q-Sepharose, SP-Sepharose and FPLC-gel filtration on Superdex 75. The protein was unadsorbed on DEAE-cellulose and Q-Sepharose, but adsorbed on SP-Sepharose. The optimal pH and temperature of the purified enzyme were 10.6 and 60 °C, respectively. The enzyme was stable in the presence of 2 % (v/v) Tween 80 and 4 M urea. More than 80 % of the enzyme activity was retained in 2 % (v/v) Triton X 100, 54 % in 10 mM EDTA and 31 % in 2 % (w/v) SDS. The enzyme was strongly inhibited by phenylmethylsulfonyl fluoride (PMSF), but not inhibited by dithiothreitol (DTT), pepstatin or lima bean trypsin inhibitor suggesting that it was a serine protease but not a trypsin-like one. The protease was inhibited by Hg2+, Cu2+, and Fe3+ ions. The Km and Vmax values of the purified enzyme for casein were 8.26 mg ∙ ml-1 and 0.668 mg ∙ ml-1 ∙ min-1, respectively.
Źródło:
Acta Biochimica Polonica; 2011, 58, 2; 269-274
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The regulatory role of AtDeg5 chloroplast protease in chronological progression of principal growth stages in Arabidopsis thaliana plants
Autorzy:
Baranek, M.
Lucinski, R.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/80598.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
serine-type protease
chymotrypsin
thylakoid membrane
photosystem II
protease
chloroplast
Arabidopsis thaliana
ontogenesis
growth stage
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
New proteases of the chloroplast envelope – what do they do there?
Autorzy:
Adam, Z.
Powiązania:
https://bibliotekanauki.pl/articles/80681.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
protease
chloroplast
thylakoid
proteomics
allene oxide synthase
jasmonic acid
serine protease
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Protease purification and characterization of a serine protease inhibitor from Egyptian varieties of soybean seeds and its efficacy against Spodoptera littoralis
Autorzy:
Abd El-latif, A.O.
Powiązania:
https://bibliotekanauki.pl/articles/65779.pdf
Data publikacji:
2015
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Opis:
Serine inhibitors have been described in many plant species and are universal throughout the plant kingdom. Trypsin inhibitors are the most common type. In the present study, trypsin and chymotrypsin inhibitory activity was detected in the seed flour extracts of four Egyptian varieties of soybean (Glycine max). The soybean variety, Giza 22, was found to have higher trypsin and chymotrypsin inhibitory potential compared to other tested soybean varieties. For this reason, Giza 22 was selected for further purification studies which used ammonium sulphate fractionation and DEAE-Sephadex A-25 column. Soybean purified proteins showed a single band on SDS-PAGE corresponding to a molecular mass of 17.9 kDa. The purified inhibitor was stable at temperatures below 60°C and was active at a wide range of pH, from 2 to 12 pH. The kinetic analysis revealed a non-competitive type of inhibition against trypsin and chymotrypsin enzymes. The inhibitor constant (Ki) values suggested that the inhibitor has higher affinity toward a trypsin enzyme than to a chymotrypsin enzyme. Purified inhibitor was found to have deep and negative effects on the mean larval weight, larval mortality, pupation, and mean pupal weight of Spodoptera littoralis. It may be concluded, that soybean protease inhibitor gene(s) could be potential targets for those future studies which are concerned with developing insect resistant transgenic plants.
Źródło:
Journal of Plant Protection Research; 2015, 55, 1
1427-4345
Pojawia się w:
Journal of Plant Protection Research
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Three Pseudomonas aeruginosa strains with different protease profiles
Autorzy:
Andrejko, Mariola
Zdybicka-Barabas, Agnieszka
Janczarek, Monika
Cytryńska, Małgorzata
Powiązania:
https://bibliotekanauki.pl/articles/1039614.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
aprA
alkaline protease
extracellular proteases
elastase B
virulence
lasB
Pseudomonas aeruginosa
Opis:
The proteolytic activity of three Pseudomonas aeruginosa strains, ATCC 27853 - a reference strain, and two clinical isolates was tested. The activity was examined after culturing the bacteria in two different growth media: the minimal M9 medium and rich Luria-Bertani broth (LB). Based on zymograms and protease activity specific assays, it was concluded that the reference strain produced three proteolytic enzymes in the LB medium: protease IV, elastase B and elastase A, while alkaline protease was only produced in the M9 medium. The clinical isolates of P. aeruginosa produced elastase B and alkaline protease when grown in the LB medium and the minimal M9 medium, respectively. PCR analysis confirmed the presence of both the lasB gene encoding elastase B and aprA coding for alkaline protease in the genomes of the three P. aeruginosa strains analyzed. The expression of these genes coding for two important P. aeruginosa virulence factors was dependent on the growth conditions in all the strains studied. The contribution of the extracellular proteinases to the virulence of P. aeruginosa strains used in this study was investigated using an insect model, the greater wax moth Galleria mellonella.
Źródło:
Acta Biochimica Polonica; 2013, 60, 1; 83-90
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Downregulation of chloroplast protease AtDeg5 leads to changes in chronological progression of ontogenetic stages, leaf morphology and chloroplast ultrastructure in Arabidopsis
Autorzy:
Baranek, M.
Wyka, T.P.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/57852.pdf
Data publikacji:
2015
Wydawca:
Polskie Towarzystwo Botaniczne
Tematy:
chloroplast protease
AtDeg5 protease
chronological progression
ontogenetic stage
leaf morphology
chloroplast ultrastructure
Arabidopsis
starch grain
Opis:
The chloroplast protein AtDeg5 is a serine-type protease peripherally attached to thylakoid membrane at its lumenal side. Since reliable data regarding the role of AtDeg5 in controlling the course of growth and developmental processes are extremely limited, two independent T-DNA insertional lines with different extent of AtDeg5 reduction were prepared and ontogenesis stage-based analysis performed. Both mutant lines displayed a compensatory overaccumulation of AtDeg8. The repression of AtDeg5 protease altered a range of phenotypic features in at least one of the mutants, with the most prominent being changes in chronological progression of development and growth of individual rosette leaves, flower production and silique ripening as well as in the area of fully expanded leaves and chloroplast ultrastructure. By analyzing the results of parallel-mutant screening we conclude that AtDeg8 overdose may rescue 23% of AtDeg5 deficiency with regard to some AtDeg5-controlled traits; alternatively AtDeg5 may have catalytic sites in excess so that these traits might remain unaltered when AtDeg5 pool is reduced by 23%. For some other AtDeg5-dependent traits the absence of excessive amount of AtDeg5 catalytic sites, lack of AtDeg5 dosage effect and inability of AtDeg8 to compensate deficiency or absence of AtDeg5 occurred.
Źródło:
Acta Societatis Botanicorum Poloniae; 2015, 84, 1
0001-6977
2083-9480
Pojawia się w:
Acta Societatis Botanicorum Poloniae
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
AtDeg2 - a chloroplast protein with dual protease/chaperone activity
Autorzy:
Jagodzik, P.
Adamiec, M.
Jackowski, G.
Powiązania:
https://bibliotekanauki.pl/articles/57301.pdf
Data publikacji:
2014
Wydawca:
Polskie Towarzystwo Botaniczne
Tematy:
chloroplast protein
protease
proteolytic enzyme
chaperone
enzyme activity
chloroplast
PDZ domain
Opis:
Chloroplast protease AtDeg2 (an ATP-independent serine endopeptidase) is cytosolically synthesized as a precursor, which is imported into the chloroplast stroma and deprived of its transit peptide. Then the mature protein undergoes routing to its functional location at the stromal side of thylakoid membrane. In its linear structure AtDeg2 molecule contains the protease domain with catalytic triad (HDS) and two PDZ domains (PDZ1 and PDZ2). In vivo AtDeg2 most probably exists as a supposedly inactive haxamer, which may change its oligomeric stage to form active 12-mer, or 24-mer. AtDeg2 has recently been demonstrated to exhibit dual protease/chaperone function. This review is focused on the current awareness with regard to AtDeg2 structure and functional significance.
Źródło:
Acta Societatis Botanicorum Poloniae; 2014, 83, 3
0001-6977
2083-9480
Pojawia się w:
Acta Societatis Botanicorum Poloniae
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Immobilization of Bacillus megaterium in Carrageenan from Maluku Sea and Their Effect on Protease Production
Autorzy:
Hamdani, Syarif
Nurlatifah, Sri
Astriany, Dewi
Singgih, Marlia W.
Ibrahim, Slamet W.
Powiązania:
https://bibliotekanauki.pl/articles/1811540.pdf
Data publikacji:
2020
Wydawca:
Politechnika Koszalińska. Wydawnictwo Uczelniane
Tematy:
carrageenan
immobilization
protease activity
Bacillus megaterium
Opis:
Bacteria immobilized in carrageenan are widely used in industry to facilitate bacterial handling and storage. Carrageenan is derived from seaweed and its nature is influenced by the condition of the origin of the sea where seaweed grows, one of the Indonesia sea territories that has seaweed that contains caraganen with good properties is Maluku. This study was conducted to determine the effect of storage time of bacteria immobilized in Maluku sea’s carrageenan on proteolytic activity, the bacteria used were Bacillus megaterium. Bacterial immobilization of carrageenan was made at concentrations of 1%, 1.5%, and 2%, storage in cold conditions for up to 9 months. Protease activity was tested using Kunitz method by adding casein as a substrate. The optimal concentration of carrageenan for immobilization of Bacillus megaterium was obtained at a concentration of 1.5%. Protease isolated from immobilized Bacillus megaterium showed increased activity value from storage for 4 months (0.0489 Ug-1) to 7 months (0.1372 Ug-1), and decreased activity after being stored for 9 months (0.0501 Ug-1).
Źródło:
Rocznik Ochrona Środowiska; 2020, Tom 22, cz. 1; 60-69
1506-218X
Pojawia się w:
Rocznik Ochrona Środowiska
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Functional conservation between yeast and plant mitochondrial m-AAA proteases
Autorzy:
Skibior, R.
Kolodziejczak, M.
Janska, H.
Powiązania:
https://bibliotekanauki.pl/articles/80313.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
FtsH protease
bifunctional enzyme
ATPase
plant mitochondrion
yeast
AAA protease
Arabidopsis
ribosomal subunit
immunoblotting
biogenesis
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 3
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Hydroxyapatite as a support in protease immobilization process
Autorzy:
Zdarta, J.
Budzinska, K.
Kolodziejczak-Radzimska, A.
Klapiszewski, Ł.
Siwinska-Stefanska, K.
Bartczak, P.
Piasecki, A.
Maciejewski, H.
Jesionowski, T.
Powiązania:
https://bibliotekanauki.pl/articles/110452.pdf
Data publikacji:
2015
Wydawca:
Politechnika Wrocławska. Oficyna Wydawnicza Politechniki Wrocławskiej
Tematy:
hydroxyapatite
enzyme immobilization
protease
physicochemical characteristic
Opis:
Hydroxyapatite is used as a matrix for immobilization of protease from Aspergillus oryzae by a process of adsorption. The matrix obtained has the surface area of 26 m2/g and particles in the shape of flakes of diameters no greater than 650 nm. The efficiency of the proposed method was confirmed by the Fourier transform infrared spectroscopy, elemental analysis and by analysis of parameters of the pore structure of matrix and products after immobilization. On the basis of the Bradford method it was found that the greatest amount of enzyme (132 mg/g) was immobilized from a solution of initial enzyme concentration of 7 mg/cm3 after 24 h of the process.
Źródło:
Physicochemical Problems of Mineral Processing; 2015, 51, 2; 633-646
1643-1049
2084-4735
Pojawia się w:
Physicochemical Problems of Mineral Processing
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Charakterystyka biochemiczna proteazy syntetyzowanej przez Streptomyces rimosus
Characterization of the protease synthesized by Streptomyces rimosus
Autorzy:
Jankiewicz, U.
Koblak, S.
Wierzchowski, P.
Russel, S.
Powiązania:
https://bibliotekanauki.pl/articles/338007.pdf
Data publikacji:
2018
Wydawca:
Instytut Technologiczno-Przyrodniczy
Tematy:
enzymy proteolityczne
inhibitory proteaz
optimum temperaturowe
promieniowce
Actinomycetes
protease inhibitors
proteolytic enzymes
temperature optimum
Opis:
Badania prezentowane w niniejszej pracy miały na celu charakterystykę biochemiczną zewnątrzkomórkowej proteazy syntetyzowanej przez wyizolowany z gleby szczep Streptomyces rimosus i ocenę możliwości praktycznego wykorzystania tego enzymu w przemyśle. Badany enzym wyizolowano z 7-dniowych hodowli bakterii Streptomyces rimosus. Oczyszczony dwukrotnie enzym wykorzystano do charakterystyki biochemicznej w zakresie optymalnych warunków jego działania oraz wpływu aktywatorów i inhibitorów. Proteaza syntetyzowana przez S. rimosus wykazywała najwyższą aktywność w temperaturze 50°C i pH 7,5 oraz wysoką termostabilność w temperaturze 50°C. Dwuwartościowe jony Zn, Mo, Ni, Cd, Co hamowały aktywność enzymu, natomiast Ca i Mg – aktywowały. Silna inhibicja aktywności enzymu w obecności diizopropylofluorofosforanu (DFP) świadczy o tym, że jest to proteaza serynowa. Aktywność badanego enzymu była stabilna w obecności takich detergentów, jak Triton X-100, Tween 20, Tween 80, bromek heksadecylotrimetyloamoniowy (CTAB) oraz dodecylosiarczanu sodu (SDS).
The research was aimed at isolation and biochemical characterization of the extracellular protease synthesized by the soil Streptomyces rimosus and assessment of the possibilities of practical use of this enzyme in the industry. For this purpose, the test enzyme was isolated from 7 day old culture of S. rimosus. The enzyme two-fold purified was used for biochemical characterization for optimal temperature and pH of activity and activators and inhibitors of activity. The S. rimosus protease showed the highest activity at 50°C and at pH 7.5 and high thermostability at 50°C. Divalent ions such as Zn, Mo, Ni, Cd, Co caused inhibition while Ca and Mg stimulated activity. Strong inhibition of activity in the presence of diisopropylfluorophosphate (DFP) indicates that it is a serine protease. The activity of the test enzyme was stable in the presence of such detergents as Triton X-100, Tween 20, Tween 80, hexadecyl trimethyl ammonium bromide (CTAB) and sodium dodecyl sulfate (SDS).
Źródło:
Woda-Środowisko-Obszary Wiejskie; 2018, 18, 2; 5-14
1642-8145
Pojawia się w:
Woda-Środowisko-Obszary Wiejskie
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel alkaline protease with antiproliferative activity from fresh fruiting bodies of the toxic wild mushroom Amanita farinosa
Autorzy:
Sun, Jian
Zhao, Yongchang
Chai, Hongmei
Wang, Hexiang
Ng, Tzi
Powiązania:
https://bibliotekanauki.pl/articles/1039854.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
alkaline protease
fruiting bodies
purification
mushroom
antiproliferative
Amanita farinosa
Opis:
A novel protease with a molecular mass of 15 kDa was purified from fresh fruiting bodies of the wild mushroom Amanita farinosa. The purification protocol entailed anion exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, cation exchange chromatography on SP-Sepharose, and gel filtration by fast protein liquid chromatography on Superdex 75. The protease was unadsorbed on DEAE-cellulose but adsorbed on Affi-gel blue gel and SP-Sepharose. It demonstrated a single 15-kDa band in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS/PAGE) and a 15-kDa peak in gel filtration. The optimal pH and optimal temperature of the protease were pH 8.0 and 65 °C, respectively. Proliferation of human hepatoma HepG2 cells was inhibited by the protease with an IC50 of 25 µM. The protease did not have antifungal or ribonuclease activity.
Źródło:
Acta Biochimica Polonica; 2011, 58, 4; 567-572
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mitochondrial protease AtFtsH4 affects the level of oxidatively modified proteins in seeds and mitochondria of A. thaliana
Autorzy:
Czarna, M.
Smakowska, E.
Janska, H.
Powiązania:
https://bibliotekanauki.pl/articles/80803.pdf
Data publikacji:
2013
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
conference
protein carbonylation
oxidative modification
plant
life cycle
AtFtsH4 protease
seed
mitochondrion
Arabidopsis thaliana
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2013, 94, 2
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The total protein content, protein fractions and proteases activities of drone prepupae of Apis mellifera due to varrosis
Autorzy:
Żółtowska, K.
Lipiński, Z.
Dmitryjuk, M.
Powiązania:
https://bibliotekanauki.pl/articles/2146371.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Parazytologiczne
Tematy:
protease
protease activity
honey bee
drone prepupa
protein fraction
varrosis
total protein
Varroa destructor
Apis mellifera
protein content
Opis:
The proteins level and activities of acid and alkaline proteases in whole body extracts of drone prepupae of Apis mellifera naturaly infested with Varroa destructor were studied. The infested and a non-infested group did not differ significantly in their total protein content. However, some differences in protein profiles were found. A lack of three protein fractions of moderate and lower molecular weight in infested prepupae was noted. Moreover, some differences in the quantity of protein in most of the fractions were observed. The activity of acid proteases from infested prepupae was lower (p < 0.05) compared with the activity of these proteases from the non-infested one group. The infested drone had higher activity of alkaline proteases than non-infested but this difference was not statisticaly significant.
Źródło:
Wiadomości Parazytologiczne; 2005, 51, 1; 43-47
0043-5163
Pojawia się w:
Wiadomości Parazytologiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The Effect of Potassium Diformate Addition to the Growth Rate and the Activity of Protease Enzyme of Giant Gourami Fingerlings (Osphronemus goramy Lacepede, 1801)
Autorzy:
Yustiati, Ayi
Nugraha, Algi Azmi
Bioshina, Ibnu Bangkit
Andriani, Yuli
Powiązania:
https://bibliotekanauki.pl/articles/1031523.pdf
Data publikacji:
2020
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
Osphronemus goramy
giant gourami
growth
potassium diformate
protease enzyme
Opis:
This research aims to investigate the effect of adding potassium diformate to commercial feed on the increase of absolute growth rate and the activity of protease enzyme. The research was conducted from July to October 2019 in the Aquaculture Laboratory Faculty of Fisheries and Marine Sciences, Padjadjaran University. The method applied in this research was an experimental method using a Completely Randomized Design (CRD), which consists of four treatments and four replications. The treatments were: (A) without addition of Potassium diformate (control), (B) addition of Potassium diformate by 0.3%, (C) addition of Potassium diformate by 0.5%, and (D) addition Potassium diformate by 0.8%. The test fish were 300 giant gouramis with 4-6 cm in length. The containers used in this research were 16 rearing aquaria with a size of 40 30 40 cm3. The density of studied giant gourami fingerlings was 10 fish per aquarium. The rearing period was 40 days. The feeding rate was 3% from biomass. Water quality parameters (temperature, pH, and dissolved oxygen), the absolute growth rate, feed conversation ratio and survival rate were observed every 10 days. The protease enzyme activities were observed at the end of the research. Data on the absolute growth rate, feeding conversion ratio, the characteristics of protease enzyme and survival rate were analyzed using the Analysis of Variance (ANNOVA) continued with Duncan’s Multiple Range Test at the level of 95%, while the water quality was analyzed descriptively. The results show that the addition of potassium diformate by 0.3% gave the best result with the absolute growth rate of 1.50%, feed conversion ratio of 2.70, protease enzyme activity by 634.2 μ/mL and survival rate of 100%.
Źródło:
World News of Natural Sciences; 2020, 32; 74-86
2543-5426
Pojawia się w:
World News of Natural Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The total protein content, protein fractions and proteases activities of drone prepupae of Apis mellifera due to varrosis
Autorzy:
Zoltowska, K
Lipinski, Z.
Dmitryjuk, M.
Powiązania:
https://bibliotekanauki.pl/articles/840749.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Parazytologiczne
Tematy:
protease
protease activity
honey bee
drone prepupa
protein fraction
varrosis
total protein
Varroa destructor
Apis mellifera
protein content
Opis:
The proteins level and activities of acid and alkaline proteases in whole body extracts of drone prepupae of Apis mellifera naturaly infested with Varroa destructor were studied. The infested and a non-infested group did not differ significantly in their total protein content. However, some differences in protein profiles were found. A lack of three protein fractions of moderate and lower molecular weight in infested prepupae was noted. Moreover, some differences in the quantity of protein in most of the fractions were observed. The activity of acid proteases from infested prepupae was lower (p < 0.05) compared with the activity of these proteases from the non-infested one group. The infested drone had higher activity of alkaline proteases than non-infested but this difference was not statisticaly significant.
Źródło:
Annals of Parasitology; 2005, 51, 1
0043-5163
Pojawia się w:
Annals of Parasitology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Binding of Aedes aegypti trypsin modulating oostatic factor [Aea-TMOF] to its receptor stimulates phosphorylation and protease processing of gut-membrane proteins
Autorzy:
Borovsky, D.
Hamdaoui, A.
Powiązania:
https://bibliotekanauki.pl/articles/55079.pdf
Data publikacji:
2008
Wydawca:
Sieć Badawcza Łukasiewicz - Instytut Przemysłu Organicznego
Tematy:
protease processing
Aedes aegypti
electrophoresis
trypsin modulating oostatic factor
phosphorylation
mosquito
insect
larva
gut-membrane protein
fluorography
gut receptor
Opis:
The binding of TMOF to its gut receptor was followed by incubating guts removed from male and female Aedes aegypti. TMOF at physiological concentrations, in the presence of [γ32P]ATP, causes phosphorylation and release of gut-membrane protein (45 kDa) that is further processed by proteolysis. In the presence of protease inhibitors only the 45 kDa protein was released. The phosphorylation and processing of the 45 kDa protein does not happen in the absence of TMOF. Both larvae and adult guts release the protein in the presence of TMOF. Male Ae. aegypti do not synthesize trypsin in their gut and do not release the 45 kDa protein in the presence of TMOF because a TMOF receptor is probably absent. Homogenized guts do not release the 45 kDa protein, indicating that the protease processing or the ecto-protein kinase activity is probably reduced after breaking the tissue. The 45 kDa phosphorylated protein can be dephosphorylated by alkaline phosphatase and protein phosphatase, indicating that the phosphate group is covalently linked to either a serine or a tyrosine moiety. This is the first report that shows that in insects, binding of a peptide hormone activates its receptor by proteolysis.
Źródło:
Pestycydy; 2008, 1-2; 13-25
0208-8703
Pojawia się w:
Pestycydy
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Znaczenie aktywności proteazy kapsydowej CP w rozwoju infekcji alfawirusowych
The role of capsid protease CP activity in the development of alphaviral infections
Autorzy:
Torzyk, Karolina
Skoreński, Marcin
Sieńczyk, Marcin
Powiązania:
https://bibliotekanauki.pl/articles/2200548.pdf
Data publikacji:
2022
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
alfawirusy
arbowirusy
proteazy serynowe
proteaza kapsydowa CP
inhibitory
alphaviruses
arboviruses
serine proteases
capsid protease CP
inhibitors
Opis:
Alphaviruses belong to the worldwide distributed Togaviridae family and Alphavirus genus. They are spherical, enveloped, single-stranded RNA arthropodborne viruses. Alphaviruses are mostly transmitted by mosquitoes (Aedes spp. and Anopheles spp.) and are geographically distributed in restricted areas where appropriate vectors are present (Fig.1.). The most recognized members of this genus are Sindbis (SINV), Semliki Forest (SFV), Venezuelan equine encephalitis (VEEV), Ross River (RRV), and Chikungunya (CHIKV) viruses. Alphaviruses are infection agents for humans and many animals. Clinically, most human infections with arthritogenic alphaviruses are associated with symptoms such as fever, headache, joint pain, rash, chronic arthritis, and encephalitis. Major events during the alphaviral infection are virus entry, replication, assembly, and budding of new virions. Alphaviral RNA encodes four nonstructural and five structural proteins. Nonstructural proteins are mainly involved in the replication process and virus pathogenesis, while structural proteins form new virions. Both groups of viral proteins are produced as single polyproteins which undergo autoproteolytic maturation. This process is carried out by the two viral proteases, cysteine protease nsP4 and C protein serine protease (CP), and is considered to be critical for virus replication. The capsid protease CP is a chymotrypsin-like serine protease with the catalytic triad including His145, Asp167, and Ser219. What is important, after a suicidal autoproteolytic event the side chain of Trp267 remains bound in a hydrophobic S1 pocket thus inhibiting further trans-proteolytic activity. Alphaviral capsid protein undergoes a single proteolytic reaction before maturation and then, after selfinactivation, it assembles to form a viral capsid shell. Inhibitors of the capsid protease have significant antiviral activity. Compounds belonging to this group can be good candidates for new antiviral drugs.
Źródło:
Wiadomości Chemiczne; 2022, 76, 5-6; 309--321
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Extrachromosomal expression of nat05 gene encoding an alkaline serine protease from Bacillus subtilis N05
Autorzy:
Thu, N.T.A.
Chau, N.T.T.
Thien, L.V.
Huy, N.D.
Khue, N.T.M.
Hung, N.B.
Luong, N.N.
Thu, L.T.A.
Loc, N.H.
Powiązania:
https://bibliotekanauki.pl/articles/80935.pdf
Data publikacji:
2018
Wydawca:
Polska Akademia Nauk. Czytelnia Czasopism PAN
Tematy:
gene encoding
serine protease
Bacillus subtilis
nat05 gene
fibrinolytic activity
alkaline serine protease
sodium dodecyl sulphate-polyacrylamide gel electrophoresis
proteolytic enzyme
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2018, 99, 4
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The use of enzymatic fungal activity in the food industry - review
Autorzy:
Drozłowska, Emilia
Powiązania:
https://bibliotekanauki.pl/articles/1076386.pdf
Data publikacji:
2019
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
amylases
enyzmes
fungi
laccase
protease
Opis:
Enzymes are increasingly used in the food industry, due to the fact that they allow to streamline many processes. They catalyse processes that require energy and are long-lasting. Mushrooms produce hydrolytic enzymes such as proteases, lipases and amylases. These enzymes are used in winemaking, brewing, confectionery and cheese production. Attempts have also been made to use paper industry enzymes such as laccase in the wine industry. The production of enzymes of animal origin is an expensive and complicated process, which is why they were interested in their production from microorganisms. This article attempts to review the current state of knowledge on the use of fungal enzymes in the food industry.
Źródło:
World Scientific News; 2019, 116; 222-229
2392-2192
Pojawia się w:
World Scientific News
Dostawca treści:
Biblioteka Nauki
Artykuł
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