scholarly journals Characterization of Cypermethrin-degradation by a Novel Molybdenum-reducing Morganella sp. Isolated from Active Agricultural Land in Northwestern Nigeria

2021 ◽  
Vol 9 (2) ◽  
pp. 25-30
Author(s):  
Mariam Lawan ◽  
Hafeez Muhammad Yakasai ◽  
Abba Babandi ◽  
Salihu Ibrahim ◽  
Dayyabu Shehu ◽  
...  
Keyword(s):  
Agricultural Land ◽  
Mineral Salt Medium ◽  
Industrial Applications ◽  
Inoculum Size ◽  
Agricultural Fields ◽  
Global Burden ◽  
Optimum Ph ◽  
Polluted Sites ◽  
Source Concentration

The increasing use of cypermethrin in agricultural fields, household and industrial applications for effective pest control had increased the global burden of the pollutant over the years. Consequently, there is an urgent need to devise techniques to eliminate this pollutant from the environment. A bacterium capable of degrading cypermethrin has been successfully screened and characterized. The bacterium was grown in a mineral salt medium (MSM) supplemented with cypermethrin as its sole carbon and energy source at an optimum pH 7.5, temperature 40 ºC, a carbon source concentration of 4 g/L, optimum incubation time of 24 h and an inoculum size of 400 µL. The potential of Morganella sp. to degrade cypermethrin makes it an important instrument for the degradation of cypermethrin. This knowledge may be useful for the optimization of environmental conditions for cypermethrin bioremediation and important for detoxification of cypermethrin polluted sites.

scholarly journals Production and Characterization of Collagenase From Bacillus sp. 6-2 Isolated From Fish Liquid Waste

2019 ◽  
Vol 12 (1) ◽  
pp. 58
Author(s):  
Sartika Danial ◽  
Hasnah Natsir ◽  
Seniwati Dali ◽  
Leliani Leliani
Keyword(s):  
Liquid Waste ◽  
Industrial Applications ◽  
Selective Medium ◽  
Bacillus Sp ◽  
Fermentation Time ◽  
Collagen Peptides ◽  
Hydrolysis Products ◽  
Native Collagen ◽  
Optimum Ph

Collagenases are enzyme that are able to hydrolyze native collagen into fragment collagen peptides. Collagenases and its hydrolysis products have received tremendous attention in medical and industrial applications. The present study was conducted to isolate and identify new collagenase producing bacteria from fish liquid waste, then produce and characterize collagenase. A total of 7 isolate from fish liquid waste were screened on selective medium containg 2 % collagen and its activity was confirmed by the formation of clear zone. Isolat 6-2 was positif as collagenase producer and identified as Bacillus sp. 6-2 by morphological and biochemical characteristics. The optimum fermentation time of enzyme was investigated. Collagenase crude extract was characterized by the effect of pH, temperature, and metal ions. Isolat 62 optimally produced collagenase enzyme after 30 h of incubation with activity of   0.072 U/mL and protein content of 3.768 mg/mL. The optimum pH and temperature were 7.0 and 40 oC, respectively. The enzyme was activated by 1 mM Ca2+and  Mg2+, and inhibited by   1 mM  Zn2+ and Co2+. Collagenase from Bacillus sp. 6-2 may have potentials for medical and industrial applications.

scholarly journals Identification and Characterization of Bacterial Lipase from Plateu Soil in West Java

2017 ◽  
Vol 18 (02) ◽  
pp. 103-108
Author(s):  
Vivitri Dewi Prasasty ◽  
Vinella Winata ◽  
Muhammad Hanafi
Keyword(s):  
Heat Stability ◽  
Industrial Applications ◽  
West Java ◽  
Ph Optimum ◽  
Good Efficiency ◽  
Optimum Ph ◽  
Glycerol Ester ◽  
Lipase Screening ◽  
Hydrolysis Of

Lipases are known as glycerol ester hydrolases that catalyze the hydrolysis of triglycerides into free fatty acids and glycerol. Lipases are found in human, animal, plant, and microorganisms. The aim of this research is to identify lipase producers and characterize bacterial lipase from West Java plateau soil. Plateau soil bacteria samples were isolated on lipase screening medium containing Rhodamine B. Olive oil was used as a substrate in screening and production medium bacterial lipases. From 16 bacterial isolate of lipase producers, 14 were identified as Bacillus sp. and the others were identified as Pseudomonas alcaligenes. All isolates were taken into production step to determine their lipase activities. Moreover, top 3 lipase activities out of 16 lipase activities were chosen to find the optimum pH and temperature. Both characterizations showed pH optimum and temperature optimum from each lipase. These optimum condition were used in heat stability characterization for each lipase samples. The result showed that lipase from isolate COK 2 in optimum pH 4 and temperature 50oC was the most stable lipase due to this sample has good and stable activity for 1 to 5 hours incubation time. Lipase sample from isolate COK 2 has good efficiency for lipase productivity in acid condition and high temperature. Results of this investigation could encourage utilization of these activity enhancers for various industrial applications.

scholarly journals Production, purification and characterization of a thermostable β-1,3-glucanase (laminarinase) produced by Moniliophthora perniciosa

2011 ◽  
Vol 83 (2) ◽  
pp. 599-609 ◽  
Author(s):  
Amanda R. Sena ◽  
Gildomar L.V. Júnior ◽  
Aristóteles Góes Neto ◽  
Alex G. Taranto ◽  
Carlos P. Pirovani ◽  
...  
Keyword(s):  
Specific Activity ◽  
Gel Filtration ◽  
Industrial Applications ◽  
Enzymatic Extract ◽  
Multivariate Statistical ◽  
Moniliophthora Perniciosa ◽  
Fermentation Time ◽  
Optimum Ph ◽  
Multivariate Statistical Approach

The enzyme glucanase from Moniliophthora perniciosa was produced in liquid medium and purified from the culture supernatant. A multivariate statistical approach (Response Surface Methodology - RSM) was employed to evaluate the effect of variables, including inducer (yeast extract) and fermentation time, on secreted glucanase activities M. perniciosa detected in the culture medium. The crude enzyme present in the supernatant was purified in two steps: precipitation with ammonium sulfate (70%) and gel filtration chromatography on Sephacryl S-200. The best inducer and fermentation time for glucanase activities were 5.9 g L-1 and 13 days, respectively. The results revealed three different isoforms (GLUI, GLUII and GLUIII) with purification factors of 4.33, 1.86 and 3.03, respectively. The partially purified enzymatic extract showed an optimum pH of 5.0 and an optimum temperature of 40°C. The enzymatic activity increased in the presence of KCl at all concentrations studied. The glucanase activity was highest in the presence of 0.2 M NaCl. The enzyme showed high thermal stability, losing only 10.20% of its specific activity after 40 minutes of incubation at 90°C. A purified enzyme with relatively good thermostability that is stable at low pH might be used in future industrial applications.

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.

Synthesis, Characterization, and Dynamic Behavior of Well-defined Dithiomaleimide-functionalized Maltodextrins

2020 ◽  
Vol 17 (2) ◽  
pp. 85-89
Author(s):  
Francisco J. Hidalgo ◽  
Nathan A.P. Lorentz ◽  
TinTin B. Luu ◽  
Jonathan D. Tran ◽  
Praveen D. Wickremasinghe ◽  
...  
Keyword(s):  
Physicochemical Properties ◽  
Dynamic Behavior ◽  
Industrial Applications ◽  
19F Nmr ◽  
Nmr Studies ◽  
Synthetic Pathway ◽  
End Groups ◽  
Sugar End

: Maltodextrins have an increasing number of biomedical and industrial applications due to their attractive physicochemical properties such as biodegradability and biocompatibility. Herein, we describe the development of a synthetic pathway and characterization of thiol-responsive maltodextrin conjugates with dithiomaleimide linkages. 19F NMR studies were also conducted to demonstrate the exchange dynamics of the dithiomaleimide-functionalized sugar end groups.

scholarly journals Bird communities in a degraded forest biodiversity hotspot of East Africa

2021 ◽  
Author(s):  
Moses Mulwa ◽  
Mike Teucher ◽  
Werner Ulrich ◽  
Jan Christian Habel
Keyword(s):  
Tropical Forests ◽  
Agricultural Land ◽  
Bird Species ◽  
Bird Communities ◽  
Natural Forest ◽  
Tree Plantations ◽  
Agricultural Fields ◽  
Degraded Forest ◽  
Forest Patches ◽  
Small Forest

AbstractTropical forests suffer severe habitat destruction. Thus, tropical forests frequently consist today of only a few small remnants that are often embedded within a matrix of agricultural fields and tree plantations. Forest specialist species have experienced severe population declines under these circumstances. We studied bird communities based on census plots set up in a near-natural forest block, as well as degraded forest patches, tree plantations, and agricultural fields, across the Taita Hills in southern Kenya. We classified each bird species according its ecology and behavior. We quantified the land cover and landscape configuration around each census plot. Typical forest species were mainly observed in the near-natural forest block, and to a lower extent in degraded forest patches. Plantations were almost devoid of birds. Bird communities of small forest fragments were more similar to that of agricultural land than the near-natural forest block. Most frugivorous, insectivorous and nectarivorous birds occurred in forest habitats, while granivorous bird species dominated the bird communities of agricultural land. The surrounding landscape had a marginal impact on bird species composition at local sites. Our study showed that the preservation of near-natural cloud forest, including small forest patches, is essential for the conservation of forest-dependent species, and that plantations do not serve as surrogate habitats.

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.

Seed and juice characterization of pomegranate fruits grown in Tunisia: Comparison between sour and sweet cultivars revealed interesting properties for prospective industrial applications

2011 ◽  
Vol 33 (2) ◽  
pp. 374-381 ◽  
Author(s):  
Nejib Hasnaoui ◽  
Messaoud Mars ◽  
Sana Ghaffari ◽  
Mokhtar Trifi ◽  
Pablo Melgarejo ◽  
...  
Keyword(s):  
Industrial Applications
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