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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 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:
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:
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:
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:
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:
Screening and characterization of thermo-active enzymes of biotechnological interest produced by thermophilic Bacillus isolated from hot springs in Tunisia
Autorzy:
Thebti, Wajdi
Riahi, Yosra
Gharsalli, Rawand
Belhadj, Omrane
Powiązania:
https://bibliotekanauki.pl/articles/1038787.pdf
Data publikacji:
2016
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
temperature
amylase
protease
cellulase
xylanase
mannanase
Geobacillus
Tunisian hot springs
Opis:
As part of the contribution to the global efforts in research of thermostable enzymes being of industrial interest, we focus on the isolation of thermophilic bacteria from Tunisian hot springs. Among the collection of 161 strains of thermophilic Bacillus isolated from different samples of thermal water in Tunisia, 20% are capable of growing at 100°C and the rest grow at 70°C or above. Preliminary activity tests on media supplemented with enzyme-substrates confirmed that 35 strains produced amylases, 37 - proteases, 43 - cellulases, 31 - xylanases and 37 - mannanases. The study of the effect of temperature on enzyme activity led to determination of the optimal temperatures of activities that vary between 60 and 100°C. Several enzymes were active at high temperatures (80, 90 and 100°C) and kept their activity even at 110°C. Several isolated strains producing enzymes with high optimal temperatures of activity were described for the first time in this study. Both strains B62 and B120 are producers of amylase, protease, cellulase, xylanase, and mannanase. The sequencing of 16S DNA identified isolated strains as Geobacillus kaustophillus, Aeribacillus pallidus, Geobacillus galactosidasus and Geobacillus toebii.
Źródło:
Acta Biochimica Polonica; 2016, 63, 3; 581-587
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Aktywnosc proteolityczna i amonifikacyjna uzytkowanych rolniczo gleb zlewni jeziora Piaseczno i Glebokie [Pojezierze Leczynsko-Wlodawskie]
Proteolytic and ammonification activity of cultivated soils of the piaseczno and glebokie catchment basin (The Leczynsko-Wlodawskie Lake District)
Autorzy:
Szwed, A
Furczak, J.
Powiązania:
https://bibliotekanauki.pl/articles/1401802.pdf
Data publikacji:
2000
Wydawca:
Polska Akademia Nauk. Instytut Agrofizyki PAN
Tematy:
Pojezierze Leczynsko-Wlodawskie
Jezioro Glebokie
jezioro Piaseczno
zlewnie jeziorne
gleby
gleby bielicowe
proteaza
aktywnosc proteolityczna
amonifikacja
aktywnosc amonifikacyjna
Leczynsko-Wlodawskie Lakeland
Lake Glebokie
Lake Piaseczno
lake catchment
soil
podzolic soil
protease
proteolytic activity
ammonification
ammonification activity
Opis:
Badania realizowano w glebie bielicowej wytworzonej z piasku luźnego, która cechuje się niewielką żyznością oraz w czarnej ziemi wytworzonej z piasku słabo gliniastego, która posiada dużą ilość części spławialnych, wysoki poziom węgla i azotu organicznego oraz znaczną pojemność sorpcyjną. Gleby te występują w sektorze rolniczym zlewni dwu jezior - Piaseczno i Głębokie (Pojezierze Łęczyńsko-Włodawskie). Próby do analiz biochemicznych pobierano 7, różnych stanowisk czterokrotnie w następujących terminach: kwiecień, maj, lipiec i wrzesień. Aktywność proteazy w glebach badano metodą Ladda i Butlera. Natomiast nasilenie procesu amonifikacji określano na podstawie przyrostu zawartości N-NH4+ (w próbkach glebowych inkubowanych z 0,1 % asparaginy) oznaczonego metodą Nesslera. Przeprowadzone badania wykazały, że aktywność proteolityczna zależała od właściwości gleby. W glebie bielicowej kształtowała się na ogół na niższym poziomie w porównaniu z czarną ziemią i była zróżnicowana w zależności od odległości stanowiska od jeziora. Potencjalna zdolność amonifikacyjna gleb nie była wyraźnie powiązana z ich właściwościami. W glebie bielicowej utrzymywała się w całym sektorze na zbliżonym poziomie. Natomiast w przypadku czarnej ziemi stwierdzono zależność badanego procesu od punktu pobrania gleby. Najwyższą wartość tej aktywności odnotowano w glebie zlokalizowanej na brzegu jeziora.
The investigations were carried out in podzolic soil of poor fertility developed from loose sand and black soil formed from slightly loamy sand with great part of fine fraction, high level of carbon and organic nitrogen and considerable sorp tivity. The soils arc located in the agricultural sector of the two lakes basin - Piaseczno and Głębokie (the Łęczyńsko-Włodawskie Lake District),The samples for biochemical analyses were gathered from different test sites for four times in the following terms: April, May, July and September, The protease activity in soils were examined after Ladd and Butler's method. Intensification of ammonification process was determined on die basis of N-NH4+ content growth (in soil samples incubated with 0,1 % asparagine) determined by Nesslef s method. The examinations proved the proteolytic activity depended on soil properties. In podzolic soil it demonstrated a lower level as compared to black soil and was differentiated in relation to test site distance off a lake. Potential ammonification activity of soils was not clearly connected with their characteristics. In podzolic .soil it maintained a similar level all over the agricultural sector, while in black soil there was stated dependence of a process examined on a sampling point. The highest value of the activity was recorded in the soil located on the lake bank.
Źródło:
Acta Agrophysica; 2000, 38; 237-246
1234-4125
Pojawia się w:
Acta Agrophysica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Bioactive metabolites produced by Spirulina subsalsa from the Baltic Sea
Autorzy:
Szubert, K.
Wiglusz, M.
Mazur-Marzec, H.
Powiązania:
https://bibliotekanauki.pl/articles/47501.pdf
Data publikacji:
2018
Wydawca:
Polska Akademia Nauk. Instytut Oceanologii PAN
Tematy:
bioactive metabolite
Spirulina subsalsa
Baltic Sea
Cyanoprokaryota
bioremediation
cytotoxic activity
liquid chromatography-tandem mass spectrometry
protease inhibitor
Źródło:
Oceanologia; 2018, 60, 3
0078-3234
Pojawia się w:
Oceanologia
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Analiza wydajności i specyficzności procesu immobilizacji syntetycznego inhibitora proteaz serynowych z zastosowaniem elektroforezy kapilarnej
Analysis of the efficiency and specificity of the synthetic serine protease inhibitor immobilization process using capillary electrophoresis
Autorzy:
Szałapata, K.
Osińska-Jaroszuk, M.
Grąz, M.
Jarosz-Wilkołazka, A.
Powiązania:
https://bibliotekanauki.pl/articles/2073100.pdf
Data publikacji:
2015
Wydawca:
Stowarzyszenie Inżynierów i Techników Mechaników Polskich
Tematy:
immobilizacja
inhibitor proteaz serynowych AEBSF
elektroforeza kapilarna
immobilization
AEBSF serine protease inhibitor
capillary electrophoresis
Opis:
Przedstawiono proces immobilizacji syntetycznego inhibitora proteaz serynowych AEBSF, który należy do rodziny związków benzosulfonowych. Zastosowanie techniki elektroforezy kapilarnej do celów analizy ilościowej pozwoliło na przeprowadzenie szybkiego pomiaru, charakteryzującego się wysoką specyficznością i precyzją. Na podstawie uzyskanych wyników stwierdzono, że inhibitor AEBSF, poddawany procesowi kowalencyjnej immobilizacji, jest efektywnie wiązany do porowatego nośnika. Jednocześnie określono, że wiąże się on z matrycą także wiązaniami adsorpcyjnymi i hydrofobowymi.
The paper describes a method of immobilization of AEBSF synthetic protease inhibitor which belongs to the family of benzensulfonyl compounds. The application of capillary electrophoresis for a quantitative analysis allows one to perform high-speed measurement characterized by high specificity and repeatability. The obtained results allowed one to confirm that the AEBSF inhibitor under covalent immobilization process is effectively bound to the porous support. It was also determined that AEBSF inhibitor binds to the matrix by adsorption and hydrophobic bonds.
Źródło:
Inżynieria i Aparatura Chemiczna; 2015, 3; 119--120
0368-0827
Pojawia się w:
Inżynieria i Aparatura Chemiczna
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:
Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli
Autorzy:
Skórko-Glonek, Joanna
Sobiecka-Szkatuła, Anna
Lipińska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1041221.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
DsbA oxidoreductase
disulfide exchange
HtrA protease
stoichiometry of HtrA-DsbA interaction
kinetics of HtrA oxidation
Opis:
DsbA is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. In the present work we provided the first detailed characterization of disulfide exchange between DsbA and its natural substrate, HtrA protease. We demonstrated that HtrA oxidation relies on DsbA, both in vivo and in vitro. We followed the disulfide exchange between these proteins spectrofluorimetrically and found that DsbA oxidizes HtrA with a 1 : 1 stoichiometry. The calculated second-order apparent rate constant (kapp) of this reaction was 3.3 × 104 ± 0.6 × 104 M-1s-1. This value was significantly higher than the values obtained for nonfunctional disulfide exchanges between DsbA and DsbC or DsbD and it was comparable to the kapp values calculated for in vitro oxidation of certain non-natural DsbA substrates of eukaryotic origin.
Źródło:
Acta Biochimica Polonica; 2006, 53, 3; 585-589
0001-527X
Pojawia się w:
Acta Biochimica Polonica
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:
Optimization and production of alkaline proteases from agro byproducts using a novel Trichoderma viridiae strain VPG 12, isolated from agro soil
Autorzy:
Shivasharanappa, K.
Hanchinalmath, J.V.
Sundeep, Y.S.
Borah, D.
Prasad Talluri, V.S.S.L.
Powiązania:
https://bibliotekanauki.pl/articles/11791.pdf
Data publikacji:
2014
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
optimization
production
alkaline protease
agricultural product
Trichoderma viride
agricultural soil
fermentation process
red gram husk
substrate
Opis:
In recent years, there has been a phenomenal increase in the use of alkaline proteases as industrial catalysts. The aim of this work was to isolate potent fungal strain from the agricultural field of Gulbarga region of India, for the production of alkaline protease by utilizing the agricultural by products viz, red and green gram and Bengal gram as substrate under submerged fermentation process. Optimization of fermentation process parameters such as substrate (Red gram husk, green gram husk and Bengal gram husk) utilization, utilization, temperature, pH and incubation period for alkaline protease production was carried out. The maximum production of alkaline protease by Trichoderma VPG 12 was found at pH 8, temperature 35 °C, incubated for 120 h. But the activity of the enzyme could also be seen in a wide range of pH (5-9) and temperature (20-40 °C). With all these properties, the strain can be considered for industrial grade production of alkaline protease.
Źródło:
International Letters of Natural Sciences; 2014, 09
2300-9675
Pojawia się w:
International Letters of Natural Sciences
Dostawca treści:
Biblioteka Nauki
Artykuł
Wyświetlanie 1-15 z 49

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