Search Results - "Delorenzi, Néstor"

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  1. 1

    Emulsifying and foaming properties of β-lactoglobulin modified by heat treatment by Moro, Andrea, Báez, Germán D., Ballerini, Griselda A., Busti, Pablo A., Delorenzi, Néstor J.

    Published in Food research international (01-04-2013)
    “…The effects of heat treatment on emulsifying properties of beta-lactoglobulin were studied in order to compare them with previous studies on foaming…”
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  2. 2

    Thermal unfolding of bovine β-lactoglobulin studied by UV spectroscopy and fluorescence quenching by Busti, Pablo, Gatti, Carlos A., Delorenzi, Néstor J.

    Published in Food research international (01-01-2005)
    “…In spite of numerous physical and biochemical studies on thermal denaturation of bovine β-lactoglobulin (β-LG), the definition of the N- and U-states, and the…”
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  3. 3

    Interaction of vitamin D3 with beta-lactoglobulin at high vitamin/protein ratios: Characterization of size and surface charge of nanoparticles by Berino, Romina P., Báez, Germán D., Ballerini, Griselda A., Llopart, Emilce E., Busti, Pablo A., Moro, Andrea, Delorenzi, Néstor J.

    Published in Food hydrocolloids (01-05-2019)
    “…Interaction between vitamin D3 with beta-lactoglobulin (β-LG) was studied by turbidimetric measurements covering vitamin concentrations up to 500 μM, within a…”
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  4. 4

    Characterization of polyphenols compounds extracted from stressed apple peel and their interaction with β-lactoglobulin by Llopart, Emilce E., Verdini, Roxana A., Delorenzi, Néstor J., Busti, Pablo A.

    Published in Heliyon (01-09-2023)
    “…This paper proposes to apply a postharvest environmental stress to red apples, Malus domestica, variety Red Delicious in order to increase the polyphenols…”
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  5. 5

    Effects of heat-treated β-lactoglobulin and its aggregates on foaming properties by Moro, Andrea, Báez, Germán D., Busti, Pablo A., Ballerini, Griselda A., Delorenzi, Néstor J.

    Published in Food hydrocolloids (01-07-2011)
    “…The effects on foaming properties of the aggregates formed by heating concentrate beta-lactoglobulin solutions (55 mg mL−1, pH 6.8) at 85 °C from 1 to 15 min…”
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    Journal Article
  6. 6

    Binding of alkylsulfonate ligands to bovine β-lactoglobulin: Effects on protein thermal unfolding by Busti, Pablo, Gatti, Carlos A., Delorenzi, Néstor J.

    Published in Food research international (01-05-2006)
    “…The effects caused by alkylsulfonate ligands (AL n ), characterized by a similar sulfonate head and a progressively longer hydrocarbon tail, on the thermal…”
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  7. 7

    Characterisation of beta‐lactoglobulin/sodium alginate dry films by Báez, Germán D., Llopart, Emilce E., Berino, Romina P., Moro, Andrea, Verdini, Roxana A., Busti, Pablo A., Delorenzi, Néstor J.

    “…Summary Optimum beta‐lactoglobulin/sodium alginate dry films (β‐LG/SA(S)) formed from casting solutions containing β‐LG 1.25% (w/v) and SA 1% (w/v) showed…”
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  8. 8

    Physicochemical Characterization of a Heat Treated Calcium Alginate Dry Film Prepared with Chicken Stock by Báez, Germán D., Piccirilli, Gisela N., Ballerini, Griselda A., Frattini, Agustín, Busti, Pablo A., Verdini, Roxana A., Delorenzi, Néstor J.

    Published in Journal of food science (01-04-2017)
    “…Solid sodium alginate was dissolved into chicken stock in order to give a final alginate concentration of 0.9 percent (w/v). Calcium ions present in chicken…”
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  9. 9

    Glycation of heat-treated β-lactoglobulin: Effects on foaming properties by Báez, Germán D., Busti, Pablo A., Verdini, Roxana, Delorenzi, Néstor J.

    Published in Food research international (01-11-2013)
    “…In this paper, the effect of glucose-glycation of beta-lactoglobulin (monomer 88%, dimer 12%) on foaming properties has been studied in 20mM phosphate buffer…”
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  10. 10

    Heat treatment of calcium alginate films obtained by ultrasonic atomizing: Physicochemical characterization by Soazo, Marina, Báez, Germán, Barboza, Andrea, Busti, Pablo A., Rubiolo, Amelia, Verdini, Roxana, Delorenzi, Néstor J.

    Published in Food hydrocolloids (01-10-2015)
    “…Planar films of calcium alginate were obtained using an ultrasonic atomizing device. Sodium alginate solutions of 0.6% and 0.9% (w/v) were nebulized with…”
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  11. 11

    Binding of alkylsulfonate ligands to bovine β-lactoglobulin: effects on protein denaturation by urea by Busti, Pablo, Scarpeci, Sonia, Gatti, Carlos A., Delorenzi, Néstor J.

    Published in Food hydrocolloids (2005)
    “…The effect of protein concentration on the interaction of alkylsulfonate ligands (AL n ), characterized by a similar sulfonate head and a progressively longer…”
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  12. 12

    Comparison between structural changes of heat-treated and transglutaminase cross-linked beta-lactoglobulin and their effects on foaming properties by Báez, Germán D., Moro, Andrea, Ballerini, Griselda A., Busti, Pablo A., Delorenzi, Néstor J.

    Published in Food hydrocolloids (01-10-2011)
    “…The main whey protein, β-lactoglobulin, was enzymatically modified by transglutaminase and analyzed for structural and conformational changes and their impact…”
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  13. 13

    Interaction of Alkylsulfonate Ligands with β-Lactoglobulin AB from Bovine Milk by Busti, Pablo, Scarpeci, Sonia, Gatti, Carlos A, Delorenzi, Néstor J

    Published in Journal of agricultural and food chemistry (01-09-1999)
    “…The interaction of alkyl sulfonate ligands (AL) with bovine β-lactoglobulin AB was measured using Trp fluorescence enhancement. One binding site per protein…”
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  14. 14

    A Simple Device to Demonstrate the Principles of Fluorometry by Delorenzi, Néstor J, Araujo, Cesar, Palazzolo, Gonzalo, Gatti, Carlos A

    Published in Journal of chemical education (01-09-1999)
    “…A simple device to demonstrate the principles of fluorimetry was constructed using low-cost components that are readily obtained. These components were a mini…”
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  15. 15

    Hydrophobicity of Whey Protein Concentrates Measured by Fluorescence Quenching and Its Relation with Surface Functional Properties by Moro, Andrea, Gatti, Carlos, Delorenzi, Néstor

    Published in Journal of agricultural and food chemistry (01-10-2001)
    “…Surface hydrophobicity of whey protein concentrate (WPC) under heated (85 °C for 5, 10, 20, 30, 40, and 60 min) and unheated conditions was measured using…”
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  16. 16

    Use of fluorescence methods to monitor unfolding transitions in β-lactoglobulin by Busti, Pablo, Scarpeci, Sonia, Gatti, Carlos, Delorenzi, Néstor

    Published in Food research international (2002)
    “…The degree of exposure of tryptophanyl residues (Trp) in beta-lactoglobulin (β-LG) molecules can be evaluated by following the external quenching of the…”
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  17. 17

    Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching by Busti, Pablo, Gatti, Carlos A, Delorenzi, Nestor J

    “…The technique of protein fluorescence quenching by acrylamide and sodium nitrite (NO 2 −) was used to study some structural aspects of β-lactoglobulin in…”
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  18. 18

    Heat Treatment of β-Lactoglobulin:  Structural Changes Studied by Partitioning and Fluorescence by Palazolo, Gonzalo, Rodríguez, Fernanda, Farruggia, Beatriz, Picó, Guillermo, Delorenzi, Néstor

    Published in Journal of agricultural and food chemistry (01-09-2000)
    “…Functional properties of whey protein concentrates (WPC) are primarily dependent on the degree of denaturation of β-lactoglobulin (β-LG), the major globular…”
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  19. 19

    Effects of heat-treated [beta]-lactoglobulin and its aggregates on foaming properties by Moro, Andrea, Baez, German D, Busti, Pablo A, Ballerini, Griselda A, Delorenzi, Nestor J

    Published in Food hydrocolloids (01-07-2011)
    “…The effects on foaming properties of the aggregates formed by heating concentrate beta-lactoglobulin solutions (55 mg mL[super]-1, pH 6.8) at 85 [deg]C from 1…”
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    Journal Article
  20. 20

    Effect of monovalent anions on type I collagen fibrillogenesis in vitro by Delorenzi, Nestor J., Sculsky, Guillermina, Gatti, Carlos A.

    “…The effect of a set of monovalent anions with different preferential binding to proteins (C1 −, Br −, I −, SCN −) on the kinetics of type I collagen…”
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