Characterization of detergent compatible protease of a halophilic Bacillus sp. EMB9: Differential role of metal ions in stability and activity

2013 ◽  
Vol 145 ◽  
pp. 357-361 ◽  
Author(s):  
Rajeshwari Sinha ◽  
S.K. Khare
Keyword(s):  
Metal Ions ◽  
Bacillus Sp ◽  
Detergent Compatible

Purification and Characterization of Thermostable α-Amylase from Soil Bacterium Bacillus sp.

2021 ◽  
Vol 28 ◽  
Author(s):  
Barış Enez
Keyword(s):  
Metal Ions ◽  
Amylase Activity ◽  
Low Cost ◽  
Sodium Dodecyl ◽  
Tween 20 ◽  
Bacillus Sp ◽  
Wide Range ◽  
Bacterium Bacillus ◽  
Triton X

Background: Amylases are used in several industrial and biotechnological sectors, including those producing textiles, detergents, paper and bakery products. Objective: This study aimed to purify an industrially important α-amylase from Bacillus sp. For this purpose, a single and rapid α-amylase purification was performed using the starch affinity method. Methods: Characterization of the purified enzyme was determined by investigating temperature, pH stability, detergents, and metal ions. Results: The purification coefficient of 29.8-fold with a yield of 9.2% was found. The molecular weight of the purified α-amylase was determined to be 53 kDa by SDS-PAGE, and thermostability was confirmed with 100% activity at 30ºC and 40ºC after 1 h. The purified enzyme was stable over a wide range of pH values, with optimum activity at pH 6.0, 7.0 and 8.0 after 2 h. The study also investigated the effects of the metal ions and detergents on the purified amylase and found that Mg2+ and Ca2+ ions were the activators of the enzyme, while Zn2+, Co2+ and Na+ ions decreased the activity. Furthermore, Hg2+ indicated complete inhibition of amylase activity. The detergents Triton X-100 and Tween 20 increased the α-amylase activity, while sodium dodecyl sulfate inhibited the activity. Conclusion: The purified α-amylase obtained from Bacillus sp. is considered to be environmentally friendly, can be processed in a short time, and has a low cost.

scholarly journals AKTIVITAS DAN KARAKTERISASI ENZIM PROTEASE ISOLAT Bacillus sp. (UJ132) SECARA KUALITATIF DAN KUANTITATIF

2019 ◽  
Vol 14 (3) ◽  
pp. 193
Author(s):  
Sumardi Sumardi ◽  
Salman Farisi ◽  
Chiristina Nugroho Ekowati ◽  
Milsa Solva Diana
Keyword(s):  
Metal Ions ◽  
Shrimp Farming ◽  
Bacillus Sp ◽  
Ph Optimum ◽  
Protease Enzyme ◽  
Protein Waste ◽  
Farming Industry ◽  
Optimum Production ◽  
Optimum Working

Bakteri penghasil enzim protease memiliki kemampuan untuk melakukan bioremediasi limbah protein. Penelitian ini dilakukan untuk mengetahui aktivitas dan karakterisasi enzim protease dari isolat Bacillus sp. (UJ132) yang diisolasi dari udang pasir (Metapenaeus affinis) di kawasan hutan mangrove Desa Margasari, Lampung Timur. Uji aktivitas enzim dilakukan secara kualitatif dan kuantitatif. Karakterisasi enzim meliputi penentuan suhu dan pH optimum, pengaruh ion logam, serta penentuan Km dan Vmaks. Dari hasil percobaan diketahui bahwa enzim protease dihasilkan pada waktu produksi optimum 18 jam dengan aktivitas protease sebesar 0,09 U/mL. Suhu optimum enzim ini yaitu pada suhu 50°C yang menghasilkan aktivitas sebesar 0,08 U/mL. Enzim protease ini mempunyai kondisi optimum pada pH 5 dengan nilai aktivitas 0,09 U/mL. Semua ion logam (Ca2+, Mn2+, Cu2+, Mg2+) berfungsi sebagai inhibitor kecuali ion Fe3+ yang berfungsi sebagai aktivator pada konsentrasi 1 mM dan 5 mM. EDTA dengan konsentrasi 1 mM dan 5 mM berfungsi sebagai inhibitor pada enzim protease isolat UJ132. Nilai Vmaks enzim protease 0,33 U/mL sedangkan Km senilai 4,59 mg/mL substrat, enzim ini mempunyai afinitas yang tinggi terhadap substrat.Shrimp farming produces protein wastes which mainly come from the remnants of given feed and excreta (feces) of shrimp. Bacteria known to possess protease enzymes have the ability to solve this protein waste problem in the shrimp farming industry. This study was conducted to determine the production and characterization of protease enzyme from Bacillus sp. (UJ132) isolated from the mangrove forest area of Margasari Village of Lampung Timur. The enzyme activity test was done qualitatively and quantitatively. The objectives of this study were to determine the optimum production of the enzymes and observe their characteristics, including determining the temperature and optimum pH, the effect of several metal ions, as well as Km and Vmax. The experimental results revealed that the protease enzyme had an optimum time of 18 hours of protease activity as much as 0.09 U/mL. The optimum temperature of this enzyme was 50°C which produced an activity of 0.08 U/mL. This protease enzyme has an optimum working condition at pH 5 with an activity value of 0.09 U/mL. All metal ions (Ca2+, Mn2+, Cu2+, Mg2+) acted as inhibitors except Fe3 + ions which acted as activators at concentrations of 1 mM and 5 mM. EDTA with a concentration of 1 mM and 5 mM served as an inhibitor of UJ132 isolate protease enzyme. The value of Vmax of the protease enzyme was 0.33 U/mL while Km was 4.59 mg/mL suggesting that this enzyme has a high affinity with the substrate.

scholarly journals Isolation and Characterization of A Bacillus Phage from Equine Carcass Disposal Site

2018 ◽  
Vol 4 (1) ◽  
pp. 61-66
Author(s):  
Taruna Anand ◽  
Nitin Virmani ◽  
Rajesh Kumar Vaid ◽  
Bidhan Chandra Bera ◽  
Umang Ahlawat ◽  
...  
Keyword(s):  
Bacillus Cereus ◽  
Disposal Site ◽  
Host Bacterium ◽  
Bacillus Sp ◽  
Carcass Disposal ◽  
Isolation And Characterization ◽  
Bacillus Phage ◽  
Group Member

Bacteriophages play an important role in bacterial control in natural niche however a little is known about Bacillus sp. phages prevailing in cadaver affected soils. In the current study, the Bacillus sp. phage was isolated from the equine cadaver disposal site and characterised to gain an insight into the issue of role of phages in biological dynamics of manure thus formed over years. Firstly, the host bacterium was isolated and identified as Bacillus cereus group member as assessed by phylogenetic analysis and secondly it’s corresponding phage from same soil sample was also enriched and characterised. The phage (VTCCBPA38) was found to belong to family Myoviridae and was active within the temperature range of 4°C - 45°C. As assessed by biological sensitivity by spot test, the phage was active against 6/19 (31.6 %) Bacilli tested including Bacillus cereus from goat mastitis. Thus the phagemay find potential use in biocontrol of diseases caused by Bacillus sp. Furthermore, this report is valuable as the first study for investigation of Bacillus sp. phage in carcass burial sites.

Digital x-ray mapping of nanometer-size supported bimetallic catalysts

1988 ◽  
Vol 46 ◽  
pp. 530-531
Author(s):  
L. T. Germinario
Keyword(s):  
Background Radiation ◽  
Metal Cluster ◽  
Single Element ◽  
Beam Diameter ◽  
X Rays ◽  
X Ray ◽  
Major Interest ◽  
Induced Changes

Understanding the role of metal cluster composition in determining catalytic selectivity and activity is of major interest in heterogeneous catalysis. The electron microscope is well established as a powerful tool for ultrastructural and compositional characterization of support and catalyst. Because the spatial resolution of x-ray microanalysis is defined by the smallest beam diameter into which the required number of electrons can be focused, the dedicated STEM with FEG is the instrument of choice. The main sources of errors in energy dispersive x-ray analysis (EDS) are: (1) beam-induced changes in specimen composition, (2) specimen drift, (3) instrumental factors which produce background radiation, and (4) basic statistical limitations which result in the detection of a finite number of x-ray photons. Digital beam techniques have been described for supported single-element metal clusters with spatial resolutions of about 10 nm. However, the detection of spurious characteristic x-rays away from catalyst particles produced images requiring several image processing steps.

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