scholarly journals Screening and Characterization of Halophilic Bacteria With Industrial Enzymes from Salt Lake Razazah, Karbala, Iraq

2017 ◽  
Vol 14 (2) ◽  
pp. 531-539 ◽  
Author(s):  
Mushtaq T. Sh. Al-Rubaye ◽  
Mastafa H. J. Al-Musawi ◽  
Javad Fakhari ◽  
Maryam Hosseini
Keyword(s):  
Salt Lake ◽  
Halophilic Bacteria ◽  
Optimal Growth ◽  
Lipase Production ◽  
Alkaline Lipase ◽  
Commercial Enzymes ◽  
Optimum Ph ◽  
Alkaline Amylase ◽  
Rrna Sequences

ABSTRACT: A total of 218 halophilic bacterial isolates were obtained from Lake Razazah, west of Karbala, Iraq. Optimum pH and temperature were 7.5 and 37 °C, respectively. According to optimal growth at different salt concentration, the slightly halophilic bacteria were the most abundant isolates with the frequency of 68%. The isolated bacteria were screened for the production of extracellular amylase, alkaline amylase, protease, alkaline protease, lipase, alkaline lipase, pectinase and cellulase. The production of pectinase (55.8%), amylase (52.6%) and lipase (50.0%) were observed in almost half of the halophilic bacteria. Alkaline amylase and alkaline lipase production were reported in less than one third (30%) of isolates. Phylogenetic analysis16S rRNA sequences indicated that all isolates were members of eight genera of the domain Bacteria, including Bacillus, Halobacillus, Virgibacillus, Oceanobacillus, Staphylococcus, Pseudomonas, Idiomarina and Halomonas. The predominant commercial enzymes producers in current study were Halobacillus sp. K51 and Halomonas sp. K46 with the ability to produce 7 out of 8 exoenzymes. The presented data shows that despite drought, dehydration, increased concentrations of salt and contaminants, Lake Razazah represents an untapped source of halophilic bacteria biodiversity.

scholarly journals SELECTION, PRODUCTION AND CHARACTERIZATION OF BACILLUS LIPASE

2011 ◽  
Vol 14 (3) ◽  
pp. 64-72
Author(s):  
Khoa Dang Tran ◽  
Huy Quang Le ◽  
Nghiep Dai Ngo
Keyword(s):  
Bacillus Subtilis ◽  
Liquid Culture ◽  
Culture Medium ◽  
Lipase Production ◽  
Liquid Culture Medium ◽  
Optimum Ph ◽  
Active Lipase ◽  
Substrate Concentrations ◽  
Bacillus Strains

The objective of this study is to screen Bacillus strains for high lipase production; from 10 strains of Bacillus subtilis OII (BS7) has ability the best lipase production. The maximum lipase was carried out using liquid culture medium at pH 7,0, substrate concentrations 1,2% (w/w) after 3 days. The optimum pH and temperature on lipase activity were found to be pH 10,0 and 60 oC respectively. Ion Mn2+, Ca2+ are the ions remain activity; active lipase was inhibited by Cu2+ , Zn2 ; solution of SDS 0,2 % decreases 95% activity. Molecular weight of lipase production by BS7 is approximate 23,8kDa. The results are preconditions for the research on recombinant lipase by Bacillus subtilis OII.

scholarly journals Characterization of the Antibiotic Compound No. 70 Produced byStreptomycessp. IMV-70

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Lyudmila P. Trenozhnikova ◽  
Almagul K. Khasenova ◽  
Assya S. Balgimbaeva ◽  
Galina B. Fedorova ◽  
Genrikh S. Katrukha ◽  
...  
Keyword(s):  
Optimal Growth ◽  
Growth Conditions ◽  
Culture Broth ◽  
Producer Strain ◽  
New Class ◽  
New Antibiotics ◽  
Actinomycete Strain ◽  
Main Component

We describe the actinomycete strain IMV-70 isolated from the soils of Kazakhstan, which produces potent antibiotics with high levels of antibacterial activity. After the research of its morphological, chemotaxonomic, and cultural characteristics, the strain with potential to be developed further as a novel class of antibiotics with chemotherapeutics potential was identified asStreptomycessp. IMV-70. In the process of fermentation, the strainStreptomycesspp. IMV-70 produces the antibiotic no. 70, which was isolated from the culture broth by extraction with organic solvents. Antibiotic compound no. 70 was purified and separated into individual components by HPLC, TLC, and column chromatography methods. The main component of the compound is the antibiotic 70-A, which was found to be identical to the peptolide etamycin A. Two other antibiotics 70-B and 70-C have never been described and therefore are new antibiotics. The physical-chemical and biological characteristics of these preparations were described and further researched. Determination of the optimal growth conditions to cultivate actinomycete-producer strain IMV-70 and development of methods to isolate, purify, and accumulate preparations of the new antibiotic no. 70 enable us to research further the potential of this new class of antibiotics.

Immobilization and Characterization of Tannase and its Haze-removing

2009 ◽  
Vol 15 (6) ◽  
pp. 545-552 ◽  
Author(s):  
Erzheng Su ◽  
Tao Xia ◽  
Liping Gao ◽  
Qianying Dai ◽  
Zhengzhu Zhang
Keyword(s):  
Kinetic Parameter ◽  
High Activity ◽  
Green Tea ◽  
Storage Stability ◽  
Residual Activity ◽  
Black Tea ◽  
Optimum Temperature ◽  
Oolong Tea ◽  
Optimum Ph

Tannase was effectively immobilized on alginate by the method of crosslinking-entrapment-crosslinking with a high activity recovery of 76.6%. The properties of immobilized tannase were investigated. Its optimum temperature was determined to be 35 ° C, decreasing 10 °C compared with that of free enzyme, whereas the optimum pH of 5.0 did not change. The thermal and pH stabilities of immobilized tannase increased to some degree. The kinetic parameter, Km, for immobilized tannase was estimated to be 11.6 × 10-4 mol/L. Fe2+ and Mn2+ could activate the activity of immobilized tannase. The immobilized tannase was also applied to treat the tea beverage to investigate its haze-removing effect. The content of non-estern catechins in green tea, black tea and oolong tea increased by 52.17%, 12.94% and 8.83%, respectively. The content of estern catechins in green tea, oolong tea and black tea decreased by 20.0%, 16.68% and 5.04%, respectively. The anti-sediment effect of green tea infusion treated with immobilized tannase was significantly increased. The storage stability and reusability of the immobilized tannase were improved greatly, with 72.5% activity retention after stored for 42 days and 86.9% residual activity after repeatedly used for 30 times.

scholarly journals Purification and Characterization of Asparaginase fromPhaseolus vulgarisSeeds

2015 ◽  
Vol 2015 ◽  
pp. 1-6 ◽  
Author(s):  
Saleh A. Mohamed ◽  
Mohamed F. Elshal ◽  
Taha A. Kumosani ◽  
Alia M. Aldahlawi
Keyword(s):  
Acute Lymphoblastic Leukemia ◽  
Lymphoblastic Leukemia ◽  
Potential Candidate ◽  
Purification And Characterization ◽  
Apparent Homogeneity ◽  
Wide Range ◽  
Optimum Ph ◽  
Glutaminase Activity ◽  
Low Activity

L-asparaginase from bacteria has been used in treatment of acute lymphoblastic leukemia. The aim of this study was to purify and characterize L-asparaginase fromPhaseolus vulgarisseeds instead of microbial sources. L-asparaginase was purified to apparent homogeneity. The enzyme has molecular mass of 79 kDa. The purified asparaginase had very low activity toward a number of asparagine and glutamine analogues. L-asparaginase was free from glutaminase activity. Kinetic parameters, Km andVmax of purified enzyme, were found to be 6.72 mM and 0.16 μM, respectively. The enzyme had optimum pH at 8.0. The enzyme showed high stability at alkaline pH (pH 7.5–9.0) when incubated for up to 24 h. L-asparaginase had the same temperature optimum and thermal stability at 37°C. K+was able to greatly enhance the activity of asparaginase by 150% compared with other metals tested. In conclusion, L-asparaginase showed no glutaminase activity and good stability over a wide range of physiological conditions, and thus it could be used as a potential candidate for treatment of acute lymphoblastic leukemia.

scholarly journals A statistical approach for optimization of alkaline lipase production by ascidian associated—Halobacillus trueperi RSK CAS9

2015 ◽  
Vol 8 ◽  
pp. 64-71 ◽  
Author(s):  
Ramamoorthy Sathishkumar ◽  
Gnanakkan Ananthan ◽  
Kathirvel Iyappan ◽  
Chinnathambi Stalin
Keyword(s):  
Statistical Approach ◽  
Lipase Production ◽  
Alkaline Lipase
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