scholarly journals The effectiveness of Proteolytic bacteria in the leather and detergent industry isolated waste from the Modjo tannery

2021 ◽  
Author(s):  
Tayachew Desalegn ◽  
◽  
Ketema Bacha ◽  
Mesfin Tafesse ◽  
Chandran Masi ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bacillus Subtilis ◽  
Proteolytic Enzymes ◽  
Digestive Enzyme ◽  
Total Solid ◽  
Growth Conditions ◽  
Protease Production ◽  
Alkaline Proteases ◽  
Extracellular Proteases ◽  
Protease Enzyme

Protease also called proteinase or peptidase is a digestive enzyme that is categorized under proteolytic enzymes and it has great potential in industrial application. Extracellular proteases are used in a variety of industries because they exhibit practically all of the characteristics needed for biotech applications such as detergent, bioremediation, food, and leather processing. In the synthesis of all three major types of acidic, neutral, and alkaline proteases, microbial sources have dominated an unbeatable area. Alkaline proteases are a large group of industrial enzymes formed by a wide variety of species, including animals, fungi, and bacteria. The fermentation method serves to make bacteria, fungi, and yeast alkaline proteases. Proteases are produced in large quantities by Gram-positive bacteria, especially those belonging to the Bacillus genus. Following standard procedures, the bacterial isolates PMOJ-01 and PMOJ-05 with the prominent zone of clearance and efficient enzyme development were further characterized to the genus level. Moreover, the growth conditions for the highest protease production were optimized with different pH, temperatures, and NaCl concentrations, in the results of PMOJ-01 and PMOJ- 05 pH (7 and 8), temperatures 45oC, and 1% NaCl concentrations both cases respectively. The proteases activities from PMOJ-01, Pseudomonas aeruginosa, and PMOJ-05, Bacillus subtilis were most active at pH 7.0 and pH 8.0 and temperature at 35oC and 45oC, respectively. The enzyme activity and the total solid protease sample of the crude enzyme of Pseudomonas aeruginosa and Bacillus subtilis were 0.299 U/ mL and 0.289 U/ mL, 1.37±0.14 U/mg, and 1.199 U/mg respectively. The effect on dehairing, distaining, and scum removal revealed that the purified protease enzyme of PMOJ-01 and PMOJ-05 can be used in detergent and leather industries.

scholarly journals Keratinolytic Protease Production by Bacillus Cereus Strain Ps03 under Submerged Fermentation: Optimization and Characterization

2016 ◽  
Vol 4 (3) ◽  
pp. 397-401
Author(s):  
M.D. BalaKumaran ◽  
R. Santhi
Keyword(s):  
Bacillus Subtilis ◽  
Scale Up ◽  
Nitrogen Sources ◽  
Maximum Activity ◽  
Protease Production ◽  
Subtilis Strain ◽  
Physical Factors ◽  
Chicken Feather ◽  
Protease Enzyme ◽  
Keratinolytic Protease

In the present study, chicken feather powder was screened for its application as the substrate for the production of keratinolytic protease by Bacillus subtilis strain PS03. Bacillus subtilis produced a high level of keratinolytic protease using chicken feather powder as substrate. With feather powder as substrate, physical factors such as incubation time, pH and temperature were optimized for increased keratinolytic protease production by Bacillus subtilis. The enzyme production was enhanced when using maltose as carbon source and yeast extract as nitrogen sources. SDS-PAGE analysis indicated the molecular weight of 46 kDa of the partially purified keratinolytic protease. The keratinolytic protease enzyme was stable over a pH range of 6 – 9 and temperature range of 35 - 50°C with maximum activity at pH 9 and 40°C. Based on the results, the use of feather powder as substrate for keratinolytic protease production is cost effective and is easy to scale up. Considering the availability and cost, chicken feather powder is considered as an ideal substrate for keratinolytic protease production in an industrial point of view. Int J Appl Sci Biotechnol, Vol 4(3): 397-401

scholarly journals Immobilization of Pseudomonas Aeruginosa in Different Matrices for the Production of Alkaline Protease

2020 ◽  
Vol 9 (1) ◽  
pp. 956-959
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Enzymatic Activity ◽  
Alkaline Protease ◽  
Calcium Alginate ◽  
Protease Production ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Microbial Cells ◽  
Protease Enzyme

Numerous enzymes are used in various types of industries, and one such enzyme used in several of these industries is proteases. Aforementioned, industries such as dairy, detergent, leather, fermentation and several other industries are benefitted with protease enzyme. In the present study, the efficiency of protease production was studied by enriching and immobilizing several matrices by a gram negative bacteria known as Pseudomonas aeruginosa .The immobilization was carried out by four different matrices under two different concentrations of 3% and 4%.Yielded results revealed highest enzymatic activity of 240 (U/ml) in 3% calcium alginate. Still, second highest enzymatic activity of 230 (U/ml) was seen in 4% calcium alginate. On the contrary, free microbial cells showed an enzymatic activity of 100 (U/ml). The peak activities for other methods area as follows: 4% calcium alginate - 133 (U/ml), 3% agar-agar - 100 (U/ml), 4% agar-agar - 91 (U/ml), 3% Gelatin - 85 (U/ml), 4% Gelatin - 88 (U/ml) and Polyacrylamide – 104 (U/ml). The most optimum matrix for the cellular entrapment of Pseudomonas aeruginosa is seen in 3% calcium alginate for alkaline protease production.

scholarly journals Optimization Conditions of Extracellular Proteases Production from a Newly IsolatedStreptomyces PseudogrisiolusNRC-15

2012 ◽  
Vol 9 (2) ◽  
pp. 949-961 ◽  
Author(s):  
El-Sayed E. Mostafa ◽  
Moataza M. Saad ◽  
Hassan M. Awad ◽  
Mohsen H. Selim ◽  
Helmy M. Hassan
Keyword(s):  
Proteolytic Enzymes ◽  
Low Cost ◽  
Nitrogen Sources ◽  
Active Role ◽  
Culture Conditions ◽  
Protease Production ◽  
Tween 20 ◽  
Extracellular Proteases ◽  
Great Ability ◽  
Initial Ph

Microbial protease represents the most important industrial enzymes, which have an active role in biotechnological processes. The objective of this study was to isolate new strain ofStreptomycesthat produce proteolytic enzymes with novel properties and the development of the low-cost medium. An alkaline protease producer strain NRC-15 was isolated from Egyptian soil sample. The cultural, morphological, physiological characters and chemotaxonomic evidence strongly indicated that the NRC-15 strain represents a novel species of the genusStreptomyces, hence the nameStrptomyces pseudogrisiolusNRC-15. The culture conditions for higher protease production by NRC-15 were optimized with respect to carbon and nitrogen sources, metal ions, pH and temperature. Maximum protease production was obtained in the medium supplemented with 1% glucose, 1% yeast extract, 6% NaCl and 100 μmol/L of Tween 20, initial pH 9.0 at 50 °C for 96 h. The current results confirm that for this strain, a great ability to produce alkaline proteases, which supports the use of applications in industry.

scholarly journals Protease production and enzymatic soaking of salt-preserved buffalo hides for leather processing

IIOAB Letters ◽  
2014 ◽  
Vol 3 (1) ◽  
Author(s):  
V. P. Zambare ◽  
S. S. Nilegaonkar ◽  
P. P. Kanekar
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Proteolytic Enzyme ◽  
Processing Time ◽  
Enzyme Concentration ◽  
Protease Production ◽  
Water Penetration ◽  
Leather Processing ◽  
Protease Enzyme ◽  
Rsm Optimization ◽  
Hydrolysis Of

Response surface methodological (RSM) optimization of protease by Pseudomonas aeruginosa MCM B327, increased 1.3-fold activity with 1% inoculum having cell density of 27.57 x 109 cells mL-1 at pH 7, 300C and 72 h of incubation. Protease enzyme recovered from P. aeruginosa showed characteristic activities against diverse proteins of hide. Enzyme was found to be active with substrates e.g. casein, Bovine serum albumin, gelatin, elastin, haemoglobin but inactive against keratin and collagen. During leather manufacturing, non-collagenase and non-keratinase activities have advantageous in a quality leather and hair saving process, respectively. Increased proteolytic enzyme concentration (0.1-0.5%) in soaking process showed increased water penetration because of hydrolysis of albumin and elastin proteins as indicated by opened fibers in histopathological sections. These findings suggest, protease secreted by P. aeruginosa may have application in soaking operation of leather processing for minimizing harmful deharing chemicals and processing time.

scholarly journals Three Pseudomonas aeruginosa strains with different protease profiles.

2013 ◽  
Vol 60 (1) ◽  
Author(s):  
Mariola Andrejko ◽  
Agnieszka Zdybicka-Barabas ◽  
Monika Janczarek ◽  
Małgorzata Cytryńska
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Alkaline Protease ◽  
Reference Strain ◽  
Galleria Mellonella ◽  
Proteolytic Enzymes ◽  
Growth Conditions ◽  
Luria Bertani ◽  
Clinical Isolates ◽  
Pcr Analysis ◽  
Growth Media

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.

scholarly journals Protease Production from UV Mutated Bacillus subtilis

2012 ◽  
Vol 47 (1) ◽  
pp. 69-76 ◽  
Author(s):  
MG Sher ◽  
M Nadeem ◽  
Q Syed ◽  
M Irfan ◽  
S Baig
Keyword(s):  
Bacillus Subtilis ◽  
Inorganic Nitrogen ◽  
Carbon Sources ◽  
Nitrogen Sources ◽  
Fermentation Medium ◽  
Maximum Activity ◽  
Inoculum Size ◽  
Protease Production ◽  
Protease Enzyme ◽  
Uv Mutation

UV mutation of the strain has significant contributation to enhance the yield of protease enzyme from Bacillus subtilis bacteria under the  cultivation conditions in submerged fermentation. The fermentation medium used for the production of protease composed of carbon  sources 1%, organic 1% or inorganic nitrogen sources 0.5% , K2HPO4 0.2 %, CaCl2 0.04% and MgSO4 0.02 % by mutated Bacillus subtilis  G-4 under the optimum parameters which are important to induce the mutated strain to produce high units of the protease, which were  temperature 37.5°C, pH 9, inoculum size 3 % v/v, glucose 1% as carbon source and peptone 1% as nitrogen source were give the maximum  455.25 + 1.66 units of protease. The results of stability studies revealed that protease of B. subtilis G-4 was stable over a broad range  of temperature (30 to 60°C) and pH (8 to 12). However, maximum activity (155.45U/ml) was observed at temperature 50°C and pH 10.  These characteristics render its potential use in detergent industries for detergent formulation.DOI: http://dx.doi.org/10.3329/bjsir.v47i1.10725 Bangladesh J. Sci. Ind. Res. 47(1), 69-76, 2012

scholarly journals Production and partial characterization of protease from Pseudomonas aeruginosa and Bacillus subtilis isolated from domestic waste dumpsite

2021 ◽  
Vol 01 (01) ◽  
pp. 26-33
Author(s):  
Amos Ndarubu Tsado ◽  
Jiya A. Gboke ◽  
Habiba Ibrahim ◽  
David Gana ◽  
Danazumi Nathaniel ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bacillus Subtilis ◽  
Industrial Applications ◽  
Protease Production ◽  
Domestic Waste ◽  
Production Methods ◽  
Optimum Ph ◽  
Microbial Strains ◽  
Microbial Strain

Background: Microorganisms are the leading source of industrial proteases. As a result of this, researchers are searching for new microbial strain with novel characteristic for protease production. Methods: In this study, some microbial strains were isolated from a soil sample obtained from domestic waste dumpsite. The isolate was screened for protease activity using casein as substrate. The proteolytic isolates were identified and used for protease production. The optimum pH and temperature as well as kinetic parameters of the enzyme were determined to predict their suitable industrial applications. Results: Pseudomonas aeruginosa and Bacillus subtilis were identified to be active proteases producers. The optimum temperature of the Pseudomonas aeruginosa and Bacillus subtilis were both recorded at 50OC while the optimum pH of Pseudomonas aeruginosa and Bacillus subtilis were recorded at 8.0 and 9.0 respectively. The Km and Vmax of protease produced from Pseudomonas aeruginosa were 222.22U/ml and 0.625mg/ml respectively while the Km and Vmax were proteases produced from Bacillus subtilis were 135.13 U/ml and 0.402 mg/ml respectively. Conclusion: The results in this study suggest that domestic waste dumpsite could be a potential source of proteolytic isolates of novel characteristic.

scholarly journals CodY Regulates Expression of the Bacillus subtilis Extracellular Proteases Vpr and Mpr

2015 ◽  
Vol 197 (8) ◽  
pp. 1423-1432 ◽  
Author(s):  
Giulia Barbieri ◽  
Birgit Voigt ◽  
Dirk Albrecht ◽  
Michael Hecker ◽  
Alessandra M. Albertini ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Amino Acid ◽  
Proteolytic Enzymes ◽  
Transcriptional Regulator ◽  
Extracellular Proteases ◽  
Gram Positive ◽  
Regulatory Regions ◽  
Content Type ◽  
Gram Positive Bacteria ◽  
Peptide Transporters

ABSTRACTCodY is a global transcriptional regulator in low-G+C Gram-positive bacteria that is responsive to GTP and branched-chain amino acids. By interacting with its two cofactors, it is able to sense the nutritional and energetic status of the cell and respond by regulating expression of adaptive genetic programs. InBacillus subtilis, more than 200 genes, including those for peptide transporters, intracellular proteolytic enzymes, and amino acid degradative pathways, are controlled by CodY. In this study, we demonstrated that expression of two extracellular proteases, Vpr and Mpr, is negatively controlled by CodY. By gel mobility shift and DNase I footprinting assays, we showed that CodY binds to the regulatory regions of both genes, in the vicinity of their transcription start points. Themprgene is also characterized by the presence of a second, higher-affinity CodY-binding site located at the beginning of its coding sequence. Using strains carryingvpr- ormpr-lacZtranscriptional fusions in which CodY-binding sites were mutated, we demonstrated that repression of both protease genes is due to the direct effect by CodY and that themprinternal site is required for regulation. Thevprpromoter is a rare example of a sigma H-dependent promoter that is regulated by CodY. In acodYnull mutant, Vpr became one of the more abundant proteins of theB. subtilisexoproteome.IMPORTANCECodY is a global transcriptional regulator of metabolism and virulence in low-G+C Gram-positive bacteria. InB. subtilis, more than 200 genes, including those for peptide transporters, intracellular proteolytic enzymes, and amino acid degradative pathways, are controlled by CodY. However, no role forB. subtilisCodY in regulating expression of extracellular proteases has been established to date. In this work, we demonstrate that by binding to the regulatory regions of the corresponding genes,B. subtilisCodY negatively controls expression of Vpr and Mpr, two extracellular proteases. Thus, inB. subtilis, CodY can now be seen to regulate the entire protein utilization pathway.

Mikrobizide und viruzide Aufbereitung von Dialysegeräten

2018 ◽  
Vol 22 (02) ◽  
pp. 82-89
Author(s):  
Friedrich von Rheinbaben ◽  
Oliver Riebe ◽  
Johanna Köhnlein ◽  
Sebastian Werner
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Bacillus Subtilis ◽  
Phase 3 ◽  
Aspergillus Brasiliensis

ZusammenfassungZentrales Bauteil des Genius® 90 Therapie Systems ist der sogenannte Genius-Tank, dem die frische Dialyseflüssigkeit entnommen und in den die verbrauchte Lösung nach der Dialyse zurückgeführt wird. Daher kommt der sicheren Aufbereitung des Systems eine besondere Bedeutung zu. Hierfür wird ein Aufbereitungsverfahren unter Verwendung von UV-Licht in Kombination mit einem chemischen Desinfektionsmittel angewendet. Ziel der hier beschriebenen Untersuchung war es, die Wirkungsbreite und Wirkungstiefe dieses Aufbereitungsverfahrens unter praxisnahen Phase-3-Bedingungen zu ermitteln. Dazu wurde das Gerät mit Mikroorganismen und Viren künstlich kontaminiert und die Wirkung der einzelnen Verfahrensschritte ermittelt. Im Gegensatz zu der üblichen Vorgehensweise praxisnaher Untersuchungen machen Aufbereitungsverfahren medizinischer Geräte unter Phase-3-Kriterien meist eine neuartige Arbeitsweise erforderlich – im Falle der hier vorgestellten Untersuchung sogar die Konstruktion eines speziellen Geräts zur Platzierung von Keimträgen im Genius-Tank. Im Ergebnis konnte gezeigt werden, dass bereits UV-Licht allein sowie in Kombination mit einem chemischen Desinfektionsmittel unter praxisnahen Bedingungen eine sichere Wirksamkeit gegen Bakterien (Pseudomonas aeruginosa) und bakterielle Sporen (Bacillus subtilis), Schimmelpilze (Aspergillus brasiliensis) und Viren (Murines Parvovirus) besitzt.

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