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Tytuł:
Partial characterization of proteases from Citrus sinensis fruit peel
Autorzy:
Ibraheem, Ademola Saheed
Malomo, Silvia O.
Powiązania:
https://bibliotekanauki.pl/articles/1178685.pdf
Data publikacji:
2017
Wydawca:
Przedsiębiorstwo Wydawnictw Naukowych Darwin / Scientific Publishing House DARWIN
Tematy:
Citrus sinensis
Proteases
industries
kinetic parameters
Opis:
Proteases are one of the most important enzymes that have various physiological and industrial applications. This study was carried out to purify and partially characterize proteases from Citrus sinensis fruit peel. Three active fractions of the proteases (I, II and III) were obtained. The Vmax for proteases I, II, III and pooled fraction were 185.19, 192.31, 111.11 and 163.93 U/ml with Michaelis-Menten’s constant (Km) 1.01, 0.44, 0.67 and 0.37 mg/ml respectively. The enzymes were optimally active at 40-50 °C. However, they retained activity at 60-70 °C. Protease I was stable up to 60 °C while proteases II and III retained more than 80% activity in the range of 25-70 °C. The optimal pH of proteases II and III was 7 while protease I was optimally active at pH 8. The enzymes were stable at alkaline pH especially between 6 and 9 retaining more than 60% of its activity. The stability of these enzymes at high temperature and different pH may be an indication of its potential applications in food, chemical and laundry industries.
Źródło:
World Scientific News; 2017, 67, 2; 250-264
2392-2192
Pojawia się w:
World Scientific News
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Modes of inhibition of cysteine proteases.
Autorzy:
Rzychon, Malgorzata
Chmiel, Dorota
Stec-Niemczyk, Justyna
Powiązania:
https://bibliotekanauki.pl/articles/1041496.pdf
Data publikacji:
2004
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cysteine proteases
serpins
inhibitors
cystatins
staphostatins
proteolysis
Opis:
Cysteine proteases are involved in many physiological processes and their hyperactivity may lead to severe diseases. Nature has developed various strategies to protect cells and whole organisms against undesired proteolysis. One of them is the control of proteolytic activity by inhibition. This paper presents the mechanisms underlying the action of proteinaceous inhibitors of cysteine proteinases and covers propeptides binding backwards relative to the substrate or distorting the protease catalytic centre similarly to serpins, the p35 protein binding covalently to the enzyme, and cystatins that are exosite binding inhibitors. The paper also discusses tyropins and chagasins that, although unrelated to cystatins, inhibit cysteine proteinases by a similar mechanism, as well as inhibitors of the apoptosis protein family that bind in a direction opposite to that of the substrate, similarly to profragments. Special attention is given to staphostatins, a novel family of inhibitors acting in an unusual manner.
Źródło:
Acta Biochimica Polonica; 2004, 51, 4; 861-873
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Next-generation nutraceuticals: bioactive peptides from plant proteases
Autorzy:
Matkawala, Fatema
Nighojkar, Sadhana
Nighojkar, Anand
Powiązania:
https://bibliotekanauki.pl/articles/16648148.pdf
Data publikacji:
2022
Wydawca:
Polska Akademia Nauk. Czasopisma i Monografie PAN
Tematy:
ACE inhibitory
antioxidant
bioactive peptides
nutraceuticals
papain
plant proteases
Opis:
Bioactive peptides are short and specific fragments of proteins with a wide range of biological activities that provide health benefits to the host. These natural peptides are safe and nontoxic and do not show any side effects. Nowadays, the production and characterization of bioactive peptides have been a key area of research as they show great potential as nutraceuticals and functional foods. Thus, bioactive peptides are considered next generation therapeutic agents that can replace pharmaceutical products with profound adverse effects in the near future. So far, proteolytic hydrolysis has been used as the method of choice for the large-scale production of bioactive peptides. Studies have reported that peptides with specific characteristics can be generated using a particular type of protease. Microbial proteases are the predominantly used ones because of the ease in their production and purification. However, recently, plant proteases have gained a renewed interest as they offer diversity and better specificity compared with other proteases. This review highlights the potential of plant proteases for the production of bioactive peptides and also describes the benefits of bioactive peptides as nutraceuticals.
Źródło:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology; 2022, 103, 4; 397-408
0860-7796
Pojawia się w:
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Proteazy: znaczenie, rola i oznaczanie
Proteases: significance, role and determination
Autorzy:
Tokarzewicz, A
Gorodkiewicz, E.
Powiązania:
https://bibliotekanauki.pl/articles/143075.pdf
Data publikacji:
2015
Wydawca:
Stowarzyszenie Inżynierów i Techników Przemysłu Chemicznego. Zakład Wydawniczy CHEMPRESS-SITPChem
Tematy:
proteazy
proteinazy
peptydazy
enzymy proteolityczne
nowotwór
proteases
proteinases
peptidases
proteolytic enzymes
cancer
Opis:
Proteazy są związkami, które odgrywają bardzo istotną rolę w ludzkim organizmie. Regulują one wiele procesów przebiegających także w innych żywych organizmach, również w wirusach, bakteriach i pasożytach. Ich zwiększona lub obniżona ilość może wskazywać na nieprawidłowości w orgaznizmie, takie jak: rozwój zapalenia, nowotwory, nadciśnienie. W artykule opisano najistotniejsze z ludzkich proteaz, ich znaczenie, rolę w organizmie oraz pokrótce metody oznaczania.
Proteases are compounds that play an important role in the human body. They regulate many processes inside the living organisms, also in viruses, bacteria and parasites. Their increased or decreased level may indicate irregularities in the body, such as: the development of inflammation, cancer and others like hypertension. This article describes the most important of human proteases, their significance, roles in the organism and shortly methods of determination.
Źródło:
Chemik; 2015, 69, 2; 81-88
0009-2886
Pojawia się w:
Chemik
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Charakterystyka i znaczenie proteinaz cysteinowych w procesie nowotworzenia
The characterization and importance of cysteine proteases in cancer development
Autorzy:
Młudzik, Paulina
Mirowski, Marek
Powiązania:
https://bibliotekanauki.pl/articles/1032578.pdf
Data publikacji:
2015
Wydawca:
Łódzkie Towarzystwo Naukowe
Tematy:
proteinazy cysteinowe
katepsyny
prokoagulant
nowotworowy
kancerogeneza
cysteine proteases
cathepsin
cancer procoagulant
cancerogenesis
Opis:
Cysteine proteases also known as thiol or sulfhydryl proteases are enzymes responsible for catalyzing the hydrolysis of peptide bonds in proteins. They take part in many physiological and pathological processes. Their abnormal activity can lead to a number of disease states including tumor growth. They are involved in the process of carcinogenesis at multiple levels– they participate in the invasion, transformation, angiogenesis, apoptosis and metastasis. The best characterised cysteine proteases are the lysosomal cathepsins, that belong to the papain family. So far 11 cysteine cathepsins have been identified: B, L, H, S, K, F, V, X, W, O and C. They take part in the activation of many proenzymes and prohormones, MHC–II–mediated antigen presentation, bone remodeling, reproduction and apoptosis. Research on the role of cysteine proteases in carcinogenesis showed elevated expression of mRNA or enzymatic activity of cathepsins in many human cancers, eg. breast, lung, brain, gastrointestinal tract, head and neck and melanoma. Cancer procoagulant also belongs to the group of cysteine proteases, however its structure and functions are still the subject of research for many scientists. Elevated levels of activity and concentrations of cancer procoagulant in the serum and tissues from patients with cancer disease compared to those observed in healthy people, provides the possibility of using this factor in the diagnosis of cancer. Many preclinical studies have shown that achieving a stop proliferation and reducing the metastatic potential of tumor cells is possible with the use of cysteine proteinases inhibitors. That gives great hope for the possibility of their application in anticancer therapy.
Proteinazy cysteinowe, nazywane również proteinazami tiolowymi lub sulfhydrolowymi, to enzymy odpowiedzialne za katalizowanie reakcji hydrolizy wiązań peptydowych w białkach. Biorą udział w licznych procesach fizjologicznych oraz patologicznych. Ich nieprawidłowa aktywność może prowadzić do wielu stanów chorobowych, w tym rozwoju nowotworów. Zaangażowane są one w proces kancerogenezy na wielu poziomach – uczestniczą w inwazji, transformacji nowotworowej, angiogenenezie, apoptozie i powstawaniu przerzutów. Najlepiej scharakteryzowanymi proteinazami cysteinowymi są, należące do rodziny papainy, lizosomalne katepsyny. Dotychczas poznano 11 ludzkich katepsyn cysteinowych: B, L, H, S, K, F, V, X, W, O i C. Biorą one udział w aktywacji wielu proenzymów i prohormonów, pośredniczą w prezentacji antygenu MHC–II, przebudowie kości, procesie reprodukcji oraz apoptozie. Badania nad udziałem proteinaz cysteinowych w procesie kancerogenezy wykazały podwyższoną ekspresję mRNA lub aktywność enzymatyczną katepsyn w wielu ludzkich nowotworach np. raku piersi, płuc, mózgu, żołądkowo–jelitowym, głowy, szyi oraz czerniaku. Do grupy proteinaz cysteinowych należy również prokoagulant nowotworowy, którego struktura, jak i pełnione przez niego funkcje są wciąż przedmiotem badań wielu naukowców. Podwyższony poziom aktywności, jak i stężenia antygenu prokoagulanta nowotworowego w surowicy krwi osób z chorobą nowotworową oraz w pooperacyjnym materiale tkankowym w stosunku do wartości obserwowanych u ludzi zdrowych, świadczy o możliwości wykorzystania tego czynnika w diagnostyce onkologicznej. Liczne badania przedkliniczne dowiodły, że zatrzymanie proliferacji oraz obniżenie potencjału metastatycznego komórek nowotworowych jest prawdopodobne przy użyciu inhibitorów proteinaz cysteinowych. Daje to duże nadzieje na możliwość zastosowania ich w terapii przeciwnowotworowej.
Źródło:
Folia Medica Lodziensia; 2015, 42, 2; 93-106
0071-6731
Pojawia się w:
Folia Medica Lodziensia
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Theoretical studies of binding modes of two covalent inhibitors of cysteine proteases.
Autorzy:
Drabik, Piotr
Politowska, Ewa
Czaplewski, Cezary
Kasprzykowski, Franciszek
Łankiewicz, Leszek
Ciarkowski, Jerzy
Powiązania:
https://bibliotekanauki.pl/articles/1044228.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cysteine proteases
covalent protease inhibitors
constrained simulated annealing
papain
molecular dynamics
Opis:
Physiological and pathological roles of cysteine proteases make them important targets for inhibitor development. Although highly potent inhibitors of this group of enzymes are known, their major drawback is a lack of sufficient specificity. Two cysteine protease covalent inhibitors, viz. (i) Z-RL-deoxo-V-peptide-epoxysuccinyl hybrid, and (ii) Z-RLVG-methyl-, have been developed and modeled in the catalytic pocket of papain, an archetypal thiol protease. A number of configurations have been generated and relaxed for each system using the AMBER force field. The catalytic pockets S3 and S4 appear rather elusive in view of the observed inhibitors' flexibility. This suggest rather limited chances for the development of selective structure-based inhibitors of thiol proteases, designed to exploit differences in the structure of catalytic pockets of various members of this family.
Źródło:
Acta Biochimica Polonica; 2000, 47, 4; 1061-1066
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Immune response against HtrA proteases in children with cutaneous mastocytosis
Autorzy:
Renke, Joanna
Kędzierska-Mieszkowska, Sabina
Lange, Magdalena
Nedoszytko, Bogusław
Liberek, Anna
Plata-Nazar, Katarzyna
Renke, Marcin
Wenta, Tomasz
Żurawa-Janicka, Dorota
Skórko-Glonek, Joanna
Lipińska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1038382.pdf
Data publikacji:
2018
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
HtrA proteases
children
cutaneous mastocytosis
mast cells
Opis:
Mast cells play an important role in both, the innate and adaptive immunity, however, clonal proliferation of abnormal mast cells in various organs leads to mastocytosis. A skin variant of the disease, cutaneous mastocytosis (CM) is the most frequent form of mastocytosis in children. HtrA proteases are modulators of important cellular processes, including cell signaling and apoptosis, and are related to development of several pathologies. The above and the observation that mast cells constitutively release the HtrA1 protein, prompted us to investigate a possible involvement of the HtrA proteins in pediatric CM. Levels of the serum autoantibodies (IgG) against the recombinant HtrA proteins (HtrA1-4) in children with CM (n=36) and in healthy controls (n=62) were assayed. Anti-HtrA IgGs were detected using enzyme linked immunosorbent assay (ELISA) and Western-blotting. In the CM sera, levels of the anti-HtrA1 and anti-HtrA3 autoantibodies were significantly increased when compared to the control group, while the HtrA protein levels were comparable. No significant differences in the anti-HtrA2 IgG level were found; for the anti-HtrA4 IgGs lower levels in CM group were revealed. In healthy children, the IgG levels against the HtrA1, -3 and -4 increased significantly with the age of children; no significant changes were observed for the anti-HtrA2 IgG. Our results suggest involvement of the HtrA1 and HtrA3 proteins in pediatric CM; involvement of the HtrA4 protein is possible but needs to be investigated further. In healthy children, the autoantibody levels against HtrA1, -3 and -4, but not against HtrA2, increase with age.
Źródło:
Acta Biochimica Polonica; 2018, 65, 3; 471-478
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Structural studies of cysteine proteases and their inhibitors.
Autorzy:
Grzonka, Zbigniew
Jankowska, Elżbieta
Kasprzykowski, Franciszek
Kasprzykowska, Regina
Łankiewicz, Leszek
Wiczk, Wiesław
Wieczerzak, Ewa
Ciarkowski, Jerzy
Drabik, Piotr
Janowski, Robert
Kozak, Maciej
Jaskólski, Mariusz
Grubb, Anders
Powiązania:
https://bibliotekanauki.pl/articles/1044158.pdf
Data publikacji:
2001
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cysteine proteases
structure-activity relationship
cystatins
synthetic inhibitors
Opis:
Cysteine proteases (CPs) are responsible for many biochemical processes occurring in living organisms and they have been implicated in the development and progression of several diseases that involve abnormal protein turnover. The activity of CPs is regulated among others by their specific inhibitors: cystatins. The main aim of this review is to discuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding fragments of cystatins.
Źródło:
Acta Biochimica Polonica; 2001, 48, 1; 1-20
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The action of ten secreted aspartic proteases of pathogenic yeast Candida albicans on major human salivary antimicrobial peptide, histatin 5
Autorzy:
Bochenska, Oliwia
Rapala-Kozik, Maria
Wolak, Natalia
Aoki, Wataru
Ueda, Mitsuyoshi
Kozik, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1038755.pdf
Data publikacji:
2016
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
secreted aspartic proteases
Sap
Candida albicans
antimicrobial peptides
histatin 5
candidiasis
Opis:
Candida albicans, belonging to the most common fungal pathogens of humans, exploits many virulence factors to infect the host, of which the most important is a family of ten secreted aspartic proteases (Saps) that cleave numerous peptides and proteins, often deregulating the host's biochemical homeostasis. It was recently shown that C. albicans cells can inactivate histatin5 (His5), a salivary histidine-rich anticandidal peptide, through the hydrolytic action of Saps. However, the current data on this subject are incomplete as only four out of ten Saps have been studied with respect to hydrolytic processing of His5 (Sap2, Sap5, Sap9-10). The aim of the study was to investigate the action of all Saps on His5 and to characterize this process in terms of peptide chemistry. It was shown that His5 was degraded by seven out of ten Saps (Sap1-4, Sap7-9) over a broad range of pH. The cleavage rate decreased in an order of Sap2>Sap9>Sap3>Sap7>Sap4>Sap1>Sap8. The degradation profiles for Sap2 and Sap9 were similar to those previously reported; however, in contrast to the previous study, Sap10 was shown to be unable to cleave His5. On a long-time scale, the peptide was completely degraded and lost its antimicrobial potential but after a short period of Sap treatment several shorter peptides (His1-13, His1-17, His1-21) that still decreased fungal survival were released. The results, presented hereby, provide extended characteristics of the action of C. albicans extracellular proteases on His5. Our study contribute to deepening the knowledge on the interactions between fungal pathogens and the human host.
Źródło:
Acta Biochimica Polonica; 2016, 63, 3; 403-410
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Defense against own arms: staphylococcal cysteine proteases and their inhibitors.
Autorzy:
Dubin, Grzegorz
Powiązania:
https://bibliotekanauki.pl/articles/1043443.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
staphostatin
staphylococcus
ssp
proteinase
protease inhibitor
staphopain
Opis:
Staphylococcus aureus is a human pathogen causing a wide range of diseases. Most staphylococcal infections, unlike those caused by other bacteria are not toxigenic and very little is known about their pathogenesis. It has been proposed that a core of secreted proteins common to many infectious strains is responsible for colonization and infection. Among those proteins several proteases are present and over the years many different functions in the infection process have been attributed to them. However, little direct, in vivo data has been presented. Two cysteine proteases, staphopain A (ScpA) and staphopain B (SspB) are important members of this group of enzymes. Recently, two cysteine protease inhibitors, staphostatin A and staphostatin B (ScpB and SspC, respectively) were described in S. aureus shedding new light on the complexity of the processes involving the two proteases. The scope of this review is to summarize current knowledge on the network of staphylococcal cysteine proteases and their inhibitors in view of their possible role as virulence factors.
Źródło:
Acta Biochimica Polonica; 2003, 50, 3; 715-724
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Metody pomiarów aktywności protez tkankowych
Metody izmerenijj aktivnosti tkanevykh proteaz
Methods of measurement of tissue proteases activity
Autorzy:
Worowski, K.
Powiązania:
https://bibliotekanauki.pl/articles/2189115.pdf
Data publikacji:
1976
Wydawca:
Polskie Towarzystwo Diagnostyki Laboratoryjnej
Źródło:
Diagnostyka Laboratoryjna; 1976, 12, 5; 273-282
0867-4043
Pojawia się w:
Diagnostyka Laboratoryjna
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Changes in expression of serine proteases HtrA1 and HtrA2 during estrogen-induced oxidative stress and nephrocarcinogenesis in male Syrian hamster
Autorzy:
Zurawa-Janicka, Dorota
Kobiela, Jaroslaw
Stefaniak, Tomasz
Wozniak, Agnieszka
Narkiewicz, Joanna
Wozniak, Michał
Limon, Janusz
Lipinska, Barbara
Powiązania:
https://bibliotekanauki.pl/articles/1040768.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
17-β-estradiol
HtrA proteases
estrogen-induced carcinogenesis
oxidative stress
Opis:
Serine proteases HtrA1 and HtrA2 are involved in cellular stress response and development of several diseases, including cancer. Our aim was to examine the involvement of the HtrA proteins in acute oxidative stress response induced in hamster kidney by estrogen treatment, and in nephrocarcinogenesis caused by prolonged estrogenization of male Syrian hamster. We used semi-quantitative RT-PCR to estimate the HtrA1 and HtrA2 mRNA levels in kidney tissues, and Western blotting to monitor the amount of the HtrA proteins. Within the first five hours following estrogen administration both HtrA1 mRNA and the protein levels were increased significantly. No changes in the expression of HtrA2 were observed. This indicates that HtrA1 may be involved in the response against oxidative stress induced by estrogen treatment in hamster kidney. During prolonged estrogenization, a significant reduction of the HtrA1 mRNA and protein levels was observed after 6 months of estradiol treatment, while the expression of HtrA2 was significantly elevated starting from the third month. This suggests an involvement of the HtrA proteins in estrogen-induced nephrocarcinogenesis in hamster. Using fluorescence in situ hybridization we localized the HtrA1 gene at the qb3-4 region of Syrian hamster chromosome 2, the region known to undergo a nonrandom deletion upon prolonged estrogenization. It is possible that the reduced level of HtrA1 expression is due to this chromosomal aberration. A full-length cDNA sequence of the hamster HtrA1 gene was obtained. It codes for a 50 kDa protein which has 98 and 96% identity with mouse and human counterparts, respectively.
Źródło:
Acta Biochimica Polonica; 2008, 55, 1; 9-20
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Inactivation of α1-proteinase inhibitor by Candida albicans aspartic proteases favors the epithelial and endothelial cell colonization in the presence of neutrophil extracellular traps
Autorzy:
Gogol, Mariusz
Ostrowska, Dominika
Klaga, Kinga
Bochenska, Oliwia
Wolak, Natalia
Aoki, Wataru
Ueda, Mitsuyoshi
Kozik, Andrzej
Rapala-Kozik, Maria
Powiązania:
https://bibliotekanauki.pl/articles/1038860.pdf
Data publikacji:
2016
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Candida albicans
aspartic proteases
α1-proteinase inhibitor
elastase
neutrophil extracellular traps
inflammation
Opis:
Candida albicans, a causative agent of opportunistic fungal infections in immunocompromised patients, uses ten secreted aspartic proteases (SAPs) to deregulate the homeostasis of the host organism on many levels. One of these deregulation mechanisms involves a SAP-dependent disturbance of the control over proteolytic enzymes of the host by a system of dedicated proteinase inhibitors, with one important example being the neutrophil elastase and alpha1-proteinase inhibitor (A1PI). In this study, we found that soluble SAPs 1-4 and the cell membrane-anchored SAP9 efficiently cleaved A1PI, with the major cleavage points located at the C-terminal part of A1PI in a close vicinity to the reactive-site loop that plays a critical role in the inhibition mechanism. Elastase is released by neutrophils to the environment during fungal infection through two major processes, a degranulation or formation of neutrophil extracellular traps (NET). Both, free and NET-embedded elastase forms, were found to be controlled by A1PI. A local acidosis, resulting from the neutrophil activity at the infection sites, favors A1PI degradation by SAPs. The deregulation of NET-connected elastase affected a NET-dependent damage of epithelial and endothelial cells, resulting in the increased susceptibility of these host cells to candidal colonization. Moreover, the SAP-catalyzed cleavage of A1PI was found to decrease its binding affinity to a proinflammatory cytokine, interleukin-8. The findings presented here suggest a novel strategy used by C. albicans for the colonization of host tissues and overcoming the host defense.
Źródło:
Acta Biochimica Polonica; 2016, 63, 1; 167-175
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Produkcja enzymów proteolitycznych przez Bacillus licheniformis
Proteolytic enzymes production by Bacillus licheniformis
Autorzy:
Trusek-Hołownia, A.
Skrzypiński, A.
Powiązania:
https://bibliotekanauki.pl/articles/2070325.pdf
Data publikacji:
2009
Wydawca:
Stowarzyszenie Inżynierów i Techników Mechaników Polskich
Tematy:
produkcja enzymów
proteazy
Bacillus licheniformis
enzyme production
proteases
Opis:
Skonfrontowano wyniki badań dotyczące produkcji enzymów proteolitycznych przez Bacillus licheniformis PCM 1847 z dostępną w literaturze wiedzą i wynikami badań uzyskanymi dla rodzaju Bacillus. Przeprowadzone eksperymenty stanowią etap przygotowawczy do hodowli prowadzonej w bioreaktorze membranowym. W wielu przypadkach zagęszczenie biomasy dzięki zastosowaniu selektywnej membrany przynosi wymierne skutki. Zgodnie z naszą wiedzą, nieznane są przypadki zastosowania bioreaktora membranowego w ciągłej syntezie hydrolaz.
Results received for Bacillus licheniformis PCM 1847 were compared with the data presented in literature. The carried out experiments are the first step to prepare the culture in a membrane bioreactor. Under a high biomass concentration thanks to membrane application a lot of processes run at the high efficiency. To the best of our knowledge the membrane bioreactor has never been applied in the continuous hydro-lases production.
Źródło:
Inżynieria i Aparatura Chemiczna; 2009, 3; 119-120
0368-0827
Pojawia się w:
Inżynieria i Aparatura Chemiczna
Dostawca treści:
Biblioteka Nauki
Artykuł
Wyświetlanie 1-15 z 43

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