Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan

San Juan de la Rambla, Spain

Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan

San Juan de la Rambla, Spain

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Esteban-Torres M.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | Alvarez Y.,CSIC - Institute of Physical Chemistry "Rocasolano" | Acebron I.,CSIC - Institute of Physical Chemistry "Rocasolano" | Rivas B.D.L.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | And 5 more authors.
FEBS Letters | Year: 2012

Endogenous galactitol-1-phosphate 5-dehydrogenase (GPDH) (EC 1.1.1.251) from Escherichia coli spontaneously interacts with Ni2+-NTA matrices becoming a potential contaminant for recombinant, target His-tagged proteins. Purified recombinant, untagged GPDH (rGPDH) converted galactitol into tagatose, and d-tagatose-6-phosphate into galactitol-1-phosphate, in a Zn2+- and NAD(H)-dependent manner and readily crystallized what has permitted to solve its crystal structure. In contrast, N-terminally His-tagged GPDH was marginally stable and readily aggregated. The structure of rGPDH revealed metal-binding sites characteristic from the medium-chain dehydrogenase/reductase protein superfamily which may explain its ability to interact with immobilized metals. The structure also provides clues on the harmful effects of the N-terminal His-tag. Structured summary of protein interactions: GPDH and GPDH bind by molecular sieving (View interaction) GPDH and GPDH bind by x-ray crystallography (View interaction) GPDH and GPDH bind by cosedimentation in solution (View interaction). © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.


Lvarez Y.,CSIC - Institute of Physical Chemistry "Rocasolano" | Esteban-Torres M.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | Acebron I.,CSIC - Institute of Physical Chemistry "Rocasolano" | De Las Rivas B.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | And 3 more authors.
Acta Crystallographica Section F: Structural Biology and Crystallization Communications | Year: 2011

Q88Y25-Lacpl is an esterase produced by the lactic acid bacterium Lactobacillus plantarum WCFS1 that shows amino-acid sequence similarity to carboxyl-esterases from the hormone-sensitive lipase family, in particular the AFEST esterase from the archaeon Archaeoglobus fulgidus and the hyperthermophilic esterase EstEI isolated from a metagenomic library. N - terminally His6-tagged Q88Y25-Lacpl has been overexpressed in Escherichia coli BL21 (DE3) cells, purified and crystallized at 291 K using the hanging-drop vapour-diffusion method. Mass spectrometry was used to determine the purity and homogeneity of the enzyme. Crystals of His6-tagged Q88Y25-Lacpl were prepared in a solution containing 2.8 M sodium acetate trihydrate pH 7.0. X-ray diffraction data were collected to 2.24 Å resolution on beamline ID29 at the ESRF. The apparent crystal point group was 422; however, initial global analysis of the intensity statistics (data processed with high symmetry in space group I422) and subsequent tests on data processed with low symmetry (space group I4) showed that the crystals were almost perfectly merohedrally twinned. Most probably, the true space group is I4, with unit-cell parameters a = 169.05, b = 169.05, c = 183.62 Å. © 2011 International Union of Crystallography. All rights reserved.


Mosquera M.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | Gimenez B.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | Da Silva I.M.,Federal University of Rio Grande do Sul | Boelter J.F.,Federal University of Rio Grande do Sul | And 3 more authors.
Food Chemistry | Year: 2014

Sea bream scales were subjected to enzymatic hydrolysis with Esperase, and a peptide fraction with a molecular mass <3 kDa (F3) was isolated by ultrafiltration. F3 was encapsulated in nanoliposomes made of partially purified phosphatidylcholine (PC). Concentrations of 3.1% and 1 mg/ml for PC and F3, respectively, were established as the best entrapment protocol by response surface methodology. The liposomes entrapment efficiency and zeta potential were 74.6 ± 0.9% and -40.8 ± 0.67 mV, respectively. The liposome size ranged from 66.2 to 214 nm, with a mean diameter of 90.3 nm and a polydispersity index of 0.25. The antioxidant activity and ACE inhibitory activity of the encapsulated peptide fraction (L-F3) remained constant after 8 days at 4 C. Encapsulation preserved the biological activities of F3, and could therefore be an alternative to improve the stability of these compounds when applied to a food product. © 2014 Elsevier Ltd. All rights reserved.


Akagunduz Y.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | Mosquera M.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | Gimenez B.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | Aleman A.,Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan | And 2 more authors.
LWT - Food Science and Technology | Year: 2014

Sea bream scales and bones were used as sources of gelatin. Scales gave a higher gelatin yield than bones pretreated with HCl or Alcalase. Demineralization with EDTA was effective especially in the case of scale gelatin that showed the lowest ash content. The pretreatment of bones with HCl led to an increase in the removal of minerals. The gel strength and viscoelastic properties of sea bream scale gelatins were higher than those of bone gelatins, and only slight differences were found between gelatin extracted from bones pretreated with HCl or Alcalase, although the amino acid profile was similar in the three gelatins. The gel strength of scale gelatins was higher than that of a commercial bovine gelatin used for comparative purpose (Bloom 200-220). When the scales gelatin was hydrolyzed with Esperase, a high ACE-inhibitory activity was found in the peptide fraction below 3kDa, and the amount of this peptide fraction required to inhibit 50% of the ACE activity (IC50) was around 60μg/mL. © 2013 Elsevier Ltd.


PubMed | Instituto Ciencia Y Tecnologia Of Alimentos Y Nutricion Ictan
Type: Journal Article | Journal: FEBS letters | Year: 2012

Endogenous galactitol-1-phosphate 5-dehydrogenase (GPDH) (EC 1.1.1.251) from Escherichia coli spontaneously interacts with Ni(2+)-NTA matrices becoming a potential contaminant for recombinant, target His-tagged proteins. Purified recombinant, untagged GPDH (rGPDH) converted galactitol into tagatose, and d-tagatose-6-phosphate into galactitol-1-phosphate, in a Zn(2+)- and NAD(H)-dependent manner and readily crystallized what has permitted to solve its crystal structure. In contrast, N-terminally His-tagged GPDH was marginally stable and readily aggregated. The structure of rGPDH revealed metal-binding sites characteristic from the medium-chain dehydrogenase/reductase protein superfamily which may explain its ability to interact with immobilized metals. The structure also provides clues on the harmful effects of the N-terminal His-tag.

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