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Enhancement of biodegradation potential of catechol 1,2-dioxygenase through its immobilization in calcium alginate gel Electron. J. Biotechnol.
Guzik,Urszula; Hupert-Kocurek,Katarzyna; Marchlewicz,Ariel; Wojcieszynska,Danuta.
Background In biodegradation processes free enzymes often undergo deactivation. Thus, it is very important to obtain highly stable enzymes by different methods. Immobilization allows for successful stabilization of many multimeric enzymes by increasing the rigidity of the enzyme structure. This study aimed to evaluate some environmental factors that affect catechol 1,2-dioxygenase from Stenotrophomonas maltophilia KB2 immobilized in alginate hydrogel. The goal of the present work was to improve the functional stability of the enzyme by increasing its structural rigidity. Results Immobilization yield and expressed activity were 100% and 56%, respectively. Under the same storage conditions, the activity of the immobilized enzyme was still observed on the...
Tipo: Journal article Palavras-chave: Arenes; Entrapment; Intradiol dioxygenase; Stenotrophomonas.
Ano: 2014 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582014000200005
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Entrapment of anaerobic thermophilic and hyperthermophilic marine microorganisms in a gellan/xanthan matrix ArchiMer
Landreau, M.; Duthoit, Frederique; Claeys-bruno, M.; Vandenabeele-trambouze, O.; Aubry, T.; Godfroy, Anne; Le Blay, Gwenaelle.
Aims The aims of this study were (i) to develop a protocol for the entrapment of anaerobic (hyper)thermophilic marine micro-organisms; (ii) to test the use of the chosen polymers in a range of physical and chemical conditions and (iii) to validate the method with batch cultures. Methods and Results The best conditions for immobilization were obtained at 80°C with gellan and xanthan gums. After 5-week incubation, beads showed a good resistance to all tested conditions except those simultaneously including high temperature (100°C), low NaCl (<0∙5 mol l−1) and extreme pH (4/8). To confirm the method efficiency, batch cultures with immobilized Thermosipho sp. strain AT1272 and Thermococcus kodakarensis strain KOD1 showed an absence of detrimental effect...
Tipo: Text Palavras-chave: (hyper)thermophilic marine micro-organisms; Anaerobiosis; Entrapment; Gellan; Immobilization; Xanthan.
Ano: 2016 URL: http://archimer.ifremer.fr/doc/00332/44352/44000.pdf
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Immobilization of alpha-amylase produced by Bacillus circulans GRS 313 BABT
Dey,Gargi; Bhupinder,Singh; Banerjee,Rintu.
A maltooligosaccharide-forming amylase from B circulans GRS 313 was immobilized by entrapment in calcium alginate beads. The immobilized activity was affected by the size of the bead and bead size of 2mm was found to be most effective for hydrolysis. Kinetics constants, Km and Vmax were estimated and were found to be affected by the bead size. The catalytic activity of the enzyme was studied in presence of various starchy residues and metal ions. HgCl2, CuSO4 and FeCl3 caused inhibition of the enzyme. The reaction conditions, pH and temperature, was optimized using response surface methodology. At the optimum pH and temperature of 4.9 and 57ºC, the apparent activity was 25.6U/g of beads, resulting in almost 2-fold increase in activity. The immobilized...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Bacillus circulans GRS313; Entrapment; Maltooligosaccharide-forming amylase; Response surface methodology; Starchy residues.
Ano: 2003 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132003000200005
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Production of D-myo-inositol(1,2,4,5,6)pentakisphosphate using alginate-entrapped recombinant Pantoea agglomerans glucose-1-phosphatase BABT
Greiner,Ralf; Sajidan,.
The glucose-1-phosphatase encoding gene (agp) of Pantoea agglomerans was sequenced and heterologously expressed in Escherichia coli. The enzyme showed very high homology to periplasmatic glucose-1-phosphatases of other members of the Enterobacteriaceae family. It was isolated from transformed Escherichia coli cells in a single step in high yields (32.3 ± 1.2 mg per litre of culture) by Ni-NT agarose affinity chromatography to >95% purity as calculated from specific activity determinations. The purified glucose-1-phosphatase was entrapped in alginate beads with an entrapment efficiency of >80%. Temperature stability was enhanced as a consequence of entrapment, whereas pH dependence of enzyme activity was not affected. Maximum catalytic activity of...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Entrapment; Glucose-1-phosphatase; Myo-inositol pentakisphosphate Pantoea agglomerans; Phytase.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132008000200002
Registros recuperados: 4
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