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Dive into the research topics where Mariela Anahí Bruno is active.

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Featured researches published by Mariela Anahí Bruno.


Journal of Protein Chemistry | 2003

Hieronymain I, a new cysteine peptidase isolated from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae)

Mariela Anahí Bruno; Marcelo F. Pardo; Néstor O. Caffini; Laura María Isabel López

A new peptidase, named hieronymain I, was purified to homogeneity from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) by acetone fractionation followed by cation exchange chromatography (FPLC) on CM-Sepharose FF. Homogeneity of the enzyme was confirmed by mass spectroscopy (MALDI-TOF), isoelectric focusing, and SDS-PAGE. Hieronymain is a basic peptidase (pI > 9.3) and its molecular mass was 24,066 Da. Maximum proteolytic activity on casein (>90% of maximum activity) was achieved at pH 8.5–9.5. The enzyme was completely inhibited by E-64 and iodoacetic acid and activated by the addition of cysteine; these results strongly suggest that the isolated protease should be included within the cysteine group. The N-terminal sequence of hieronymain (ALPESIDWRAKGAVTEVKRQDG) was compared with 25 plant cysteine proteases that showed more than 50% of identity.


Food Research International | 2017

ACE-inhibitory peptides from bovine caseins released with peptidases from Maclura pomifera latex

María Alicia Corrons; Constanza Liggieri; Sebastián Alejandro Trejo; Mariela Anahí Bruno

In work reported here, a proteolytic extract prepared from Maclura pomifera latex was employed to hydrolyze bovine caseins. Densitograms of Tricine-sodium-dodecyl-sulfate-polyacrylamide-gel electrophoresis (SDS-PAGE) indicated that the caseins were considerably degraded after a 10-min reaction. The degree of hydrolysis determined by the 2,4,6-trinitrobenzenesulfonic-acid method was 17.1±0.7% after 180min of digestion. The concentration of small peptides increased with hydrolysis time, and analysis by reverse-phase high-performance liquid chromatography (RP HPLC) and mass spectrometry, revealed a virtually unchanged peptide profile. These results suggested that those proteases were highly specific, as only certain peptide bonds were cleaved. The hydrolysate of 180min displayed the highest inhibition of angiotensin-converting enzyme (ACE) showing an IC50 of 1.72±0.25mg/mL, and the analysis of the peptide fractionation in this hydrolysate by RP HPLC exhibited two peaks responsible for that activity. Fragmentation analysis through the use of iterated matrix-assisted-laser-desorption-ionization-time-of-flight mass spectrometry (MALDI-TOF/TOF MS/MS) with the aid of bioinformatics tools enabled us to deduce two peptide sequences-one, YQEPVLGPVRGPFPIIV, having been previously reported as an ACE-inhibitor; the other, RFFVAPFPE, as yet undescribed. The presence of bioactive peptides in these casein hydrolysates argues for their potential use in the development of functional foods.


Food Chemistry | 2018

Miniature cheeses made with blends of chymosin and a vegetable rennet from flowers of Silybum marianum: Enzymatic characterization of the flower-coagulant peptidase

M. Laura Colombo; Agustina Fernández; Cecilia Cimino; Constanza Liggieri; Mariela Anahí Bruno; Carlos Faro; Paula Veríssimo; Sandra Vairo-Cavalli

Binary blends of S. marianum-flower extract and chymosin, as coagulant preparations, enabled the manufacture of miniature cheeses with distinctive characteristics compared to those of chymosin-renneted cheeses. The physicochemical parameters, sensory attributes of the cheeses, and in-vitro water-soluble antioxidant activity were analyzed and compared to those properties obtained from control chymosin-renneted cheeses. The preponderant proteolytic constituent in the flower extract was isolated in a two-step-purification protocol. The thus purified aspartic peptidase was maximally active at acidic pHs and exhibited a preference for peptide bonds between hydrophobic residues. Enzymologic characterization revealed differences in the kinetic parameters and specificity compared to other enzymes employed, such as rennet. S. marianum-flower extract, as a source of peptidase with distinctive characteristics, is a suitable substitute for chymosin in miniature-cheese production. The addition of vegetable rennet contributed to the development of an intense aroma and conferred antioxidant activity to the cheeses and wheys.


Food Chemistry | 2018

Preparation of soy protein hydrolysates with antioxidant activity by using peptidases from latex of Maclura pomifera fruits

Andrea Milagros Reyes Jara; Constanza Liggieri; Mariela Anahí Bruno

A partially purified proteolytic extract prepared from Maclura pomifera latex was employed in hydrolyzing a soybean-protein isolate (4.2 mg/mL). The hydrolysis-product formation, monitored by tricine-sodium-dodecyl-sulfate-polyacrylamyde-gel electrophoresis and reverse-phase high-performance liquid chromatography, indicated that after 10 min of reaction the main soybean proteins disappeared. The maximum degree of hydrolysis was 36.2% after a 180-min digestion. The 90-min hydrolysate presented an IC50 of 31.6 ± 0.2 µg/mL, and a trolox equivalent antioxidant capacity of 157.6 and 176.9 µmoles TE per g of peptide determined by two different methods. Analysis by matrix-assisted-laser-desorption-ionization-time-of-flight mass spectrometry (MALDI-TOF MS), followed by the application of bioinformatics tools, enabled the deduction of fourteen theoretical peptide sequences containing antioxidant amino acids at >60%, none of which sequences had been previously reported as antioxidants. Finally, we consider that this 90-min hydrolysate would constitute a promising ingredient in the manufacture of functional foods.


Lwt - Food Science and Technology | 2010

Milk clotting and proteolytic activity of an enzyme preparation from Bromelia hieronymi fruits

Mariela Anahí Bruno; Cristian M. Lazza; María E. Errasti; Laura María Isabel López; Néstor O. Caffini; Marcelo F. Pardo


Lwt - Food Science and Technology | 2012

Milk clotting activity and production of bioactive peptides from whey using Maclura pomifera proteases

María Alicia Corrons; Juan Ignacio Bertucci; Constanza Liggieri; Laura María Isabel López; Mariela Anahí Bruno


Protein Journal | 2006

Isolation and characterization of hieronymain II, another peptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae).

Mariela Anahí Bruno; Sebastián A. Trejo; Xavier F. Avilés; Néstor O. Caffini; Laura María Isabel López


Journal of Molecular Catalysis B-enzymatic | 2009

Screening of plant peptidases for the synthesis of arginine-based surfactants

Susana R. Morcelle; Constanza Liggieri; Mariela Anahí Bruno; Nora Priolo; Pere Clapés


Protein Journal | 2008

Purification and Characterization of Hieronymain III. Comparison with Other Proteases Previously Isolated from Bromelia hieronymi Mez

Mariela Anahí Bruno; Sebastián A. Trejo; Néstor O. Caffini; Laura María Isabel López


Lwt - Food Science and Technology | 2015

Application of peptidases from Maclura pomifera fruit for the production of active biopeptides from whey protein

Juan Ignacio Bertucci; Constanza Liggieri; María Laura Colombo; Sandra Elizabeth Vairo Cavalli; Mariela Anahí Bruno

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Constanza Liggieri

National University of La Plata

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Néstor O. Caffini

National University of La Plata

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Marcelo F. Pardo

National University of La Plata

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Sebastián A. Trejo

Autonomous University of Barcelona

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Cecilia Cimino

National University of La Plata

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Juan Ignacio Bertucci

National University of La Plata

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María Alicia Corrons

National University of La Plata

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Agustina Fernández

National Scientific and Technical Research Council

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