4 documents found, page 1 of 1
One-step immobilization and stabilization of a recombinant Enterococcus faecium...
Sousa, Marylane de; Melo, Vânia M. M.; Hissa, Denise Cavalcante; Manzo, Ricardo M.; Mammarella, Enrique J.; Antunes, André Saraiva Leão MarceloA recombinant L-arabinose isomerase from Enterococcus faecium DBFIQ E36 was immobilized onto multifunctional epoxide supports by chemical adsorption and onto a chelate-activated support via polyhistidine-tag, located on the N-terminal (N-His-L-AI) or on the C-terminal (C-His-L-AI) sequence, followed by covalent bonding between the enzyme and the support. The results were compared to reversible L-AI immobilizati...
Thermotolerant lipase from Penicillium sp. section Gracilenta CBMAI 1583: Effec...
Turati, Daniela Flávia M. [UNESP]; Almeida, Alex F.; Terrone, Cárol C. [UNESP]; Nascimento, Juliana M.F. [UNESP]; Terrasan, César R.F.Made available in DSpace on 2019-10-06T16:05:25Z (GMT). No. of bitstreams: 0 Previous issue date: 2019-01-01; Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP); Ministerio de Ciencia e Innovación; In this study, Penicillium sp. section Gracilenta CBMAI 1583 was used to produce lipase under submerged conditions. The enzyme was purified and the biochemical properties of both the crude and purified enz...
Immobilization of lipase from Penicillium sp. section Gracilenta (CBMAI 1583) o...
Turati, Daniela F. M. [UNESP]; Morais, Wilson G.; Terrasan, César R. F.; Moreno-Perez, Sonia; Pessela, Benevides C.; Fernandez-Lorente, GloriaMade available in DSpace on 2018-12-11T17:11:16Z (GMT). No. of bitstreams: 0 Previous issue date: 2017-01-01; Lipases are promising enzymes that catalyze the hydrolysis of triacylglycerol ester bonds at the oil/water interface. Apart from allowing biocatalyst reuse, immobilization can also affect enzyme structure consequently influencing its activity, selectivity, and stability. The lipase from Penicillium sp. ...
Improving Properties of a Novel β-Galactosidase from Lactobacillus plantarum by...
Benavente, Rocio; Pessela, Benevides C.; Curiel, Jose Antonio; de las Rivas, Blanca; Muñoz, Rosario; Guisán, Jose Manuel; Mancheño, Jose M.A novel -galactosidase from Lactobacillus plantarum (LPG) was over-expressed in E. coli and purified via a single chromatographic step by using lowly activated IMAC (immobilized metal for affinity chromatography) supports. The pure enzyme exhibited a high hydrolytic activity of 491 IU/mL towards o-nitrophenyl -d-galactopyranoside. This value was conserved in the presence of different divalent cations and was qu...