Laura Lopez - Academia.edu (original) (raw)

Papers by Laura Lopez

Research paper thumbnail of Purificación de una nueva endopeptidasa aislada de frutos de Bromelia hieronymi Mez (Bromelia-ceae)

Acta Farmaceutica Bonaerense, 2002

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Research paper thumbnail of Proteases present in latex from fruits of maclura pomifera raf. schneid. moraceae

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Research paper thumbnail of Proteasas de plantas superiores ii. Ficina ( ec 3.4.22.32 )

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Research paper thumbnail of Desarrollo de procesos destinados a minimizar el impacto ambiental de las curtiembres de la provincia de Buenos Aires

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Research paper thumbnail of New purified plant proteinases for the food industry

Acta Alimentaria, 1991

A crude enzyme preparation obtained from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) s... more A crude enzyme preparation obtained from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) shows a broad pH range of optimum proteolytic activity and a good thermal stability up to 45°C. Diafiltration followed by ion-exchange chromatography allows the separation of four proteolytic components of closely related molecular weights

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Research paper thumbnail of Proteasas de plantas superiores. I. Caracteristicas generales, rol fisiologico y aplicaciones

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Research paper thumbnail of Proteasas de plantas superiores

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Research paper thumbnail of Insights into the hydrolytic activity of Asclepias fruticosa L. protease

Biotechnology Letters, 2019

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Research paper thumbnail of Structural Properties of Macrodontain I, a Cysteine Protease from Pseudananas macrodontes (Morr.) Harms (Bromeliaceae)

Applied biochemistry and biotechnology, Jan 15, 2018

The primary structure of macrodontain I, a peptidase from Pseudananas macrodontes fruits, was det... more The primary structure of macrodontain I, a peptidase from Pseudananas macrodontes fruits, was determined using Edman's degradation. The enzyme is a non-glycosylated peptidase composed by 213 amino acids with a calculated molecular weight of 23,486.18 Da, pI value 6.99, and a molar extinction coefficient at 280 nm of 61,685 M cm. The alignment of the sequence of macrodontain I with those cysteine peptidases from species belonging to the family Bromeliaceae showed the highest identity degree (87.74%) against fruit bromelain. A remarkable fact is that all these peptidase sequences show two Met contiguous residues (Met121 and 122) and the nonapeptide VPQSIDWRD located in the mature N-terminal region. Residues Cys26 and His159, which constitute the catalytic dyad in all cysteine peptidases, as well as active site residues Gln20 and Asn176, characteristic of Clan C1A, are conserved in macrodontain I. The 3-D model suggests that the enzyme belongs to the α + β class of proteins, with t...

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

LWT - Food Science and Technology, 2012

... Maria Alicia Corrons , E-mail The Corresponding Author , Juan Ignacio Bertucci , E-mail The C... more ... Maria Alicia Corrons , E-mail The Corresponding Author , Juan Ignacio Bertucci , E-mail The Corresponding Author , Constanza Silvina Liggieri , E-mail The Corresponding Author , Laura María Isabel López , E-mail The Corresponding Author , Mariela Anahí Bruno ...

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Research paper thumbnail of Purification of a new endopeptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae)

Acta Farmacéutica …, 2002

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Research paper thumbnail of Proteolytic extracts of three Bromeliaceae species as eco-compatible tools for leather industry

Environmental science and pollution research international, Jan 2, 2018

Most tanneries use high proportions of Na2S and CaO during the dehairing step, resulting in efflu... more Most tanneries use high proportions of Na2S and CaO during the dehairing step, resulting in effluents of high alkalinity and large amounts of suspended solid, besides the risk of liberating the toxic H2S. Solid waste rich in protein is another environmental problem of tanneries. Enzymes are an interesting technological tool for industry due to their biodegradability, nontoxic nature, and nonpolluting effluent generation. In the leather industry, proteases have been chosen as a promising eco-friendly alternative to Na2S/CaO dehairing. Extracts with high proteolytic activity have been obtained from fruits of Bromeliaceae species: Bromelia balansae Mez (Bb), Bromelia hieronymi Mez (Bh), and Pseudananas macrodontes (Morr.) Harms (Pm). In this work, Bb, Bh, and Pm have been studied for application in the leather industry, focusing in their dehairing properties. Enzymatic activities were measured against collagen, keratin, elastin, and epidermis while a dehairing assay was performed by em...

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Research paper thumbnail of A Bowman-Birk protease inhibitor purified, cloned, sequenced and characterized from the seeds of Maclura pomifera (Raf.) Schneid

Planta, Jan 24, 2016

A new BBI-type protease inhibitor with remarkable structural characteristics was purified, cloned... more A new BBI-type protease inhibitor with remarkable structural characteristics was purified, cloned, and sequenced from seeds of Maclura pomifera , a dicotyledonous plant belonging to the Moraceae family. In this work, we report a Bowman-Birk inhibitor (BBI) isolated, purified, cloned, and characterized from Maclura pomifera seeds (MpBBI), the first of this type from a species belonging to Moraceae family. MpBBI was purified to homogeneity by RP-HPLC, total RNA was extracted from seeds of M. pomifera, and the 3'RACE-PCR method was applied to obtain the cDNA, which was cloned and sequenced. Peptide mass fingerprinting (PMF) analysis showed correspondence between the in silico-translated protein and MpBBI, confirming that it corresponds to a new plant protease inhibitor. The obtained cDNA encoded a polypeptide of 65 residues and possesses 10 cysteine residues, with molecular mass of 7379.27, pI 6.10, and extinction molar coefficient of 9105 M(-1) cm(-1). MpBBI inhibits strongly tryp...

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Research paper thumbnail of Purification and characterization of a new plant endopeptidase isolated from latex of Asclepias fruticosa L. (Asclepiadaceae)

Journal of protein chemistry, 2001

Asclepias fruticosa L. is a small shrub containing latex with proteolytic activity. The crude ext... more Asclepias fruticosa L. is a small shrub containing latex with proteolytic activity. The crude extract (latex diluted 1:250 and ultracentrifuged) contained 276 microg of protein/mL and the proteolytic activity reached 1.2 caseinolytic U/mL. This enzyme preparation was very stable even after 2 hours at 45 degrees C, but was quickly inactivated after 5 minutes at 80 degrees C. Chromatographic purification was achieved by FPLC using a cation exchanger (SP-Sepharose FF). Thus, a unique proteolitically active fraction could be isolated, being homogeneous by bidimensional electrophoresis and mass spectrometry (Mr = 23,652). The optimum pH range was achieved at 8.5-10.5. The enzyme activity was completely inhibited by specific cysteine peptidases inhibitors. Isoelectric focusing followed by zymogram showed the enzyme had a pI greater than 9.3. The N-terminus sequence (LPDSVDWREKGVVFPIRNQGK) shows a great deal of similarity to those of the other cysteine endopeptidases isolated from latices ...

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Research paper thumbnail of A Novel Trypsin and α-Chymotrypsin Inhibitor from Maclura pomifera Seeds

Letters in Drug Design & Discovery, 2010

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

Journal of protein chemistry, 2003

A new peptidase, named hieronymain I, was purified to homogeneity from unripe fruits of Bromelia ... more 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.

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Research paper thumbnail of Sequencing and characterization of asclepain f: the first cysteine peptidase cDNA cloned and expressed from Asclepias fruticosa latex

Planta, 2009

Asclepain f is a papain-like protease previously isolated and characterized from latex of Asclepi... more Asclepain f is a papain-like protease previously isolated and characterized from latex of Asclepias fruticosa. This enzyme is a member of the C1 family of cysteine proteases that are synthesized as preproenzymes. The enzyme belongs to the alpha + beta class of proteins, with two disulfide bridges (Cys22-Cys63 and Cys56-Cys95) in the alpha domain, and another one (Cys150-Cys201) in the beta domain, as was determined by molecular modeling. A full-length 1,152 bp cDNA was cloned by RT-RACE-PCR from latex mRNA. The sequence was predicted as an open reading frame of 340 amino acid residues, of which 16 residues belong to the signal peptide, 113 to the propeptide and 211 to the mature enzyme. The full-length cDNA was ligated to pPICZalpha vector and expressed in Pichia pastoris. Recombinant asclepain f showed endopeptidase activity on pGlu-Phe-Leu-p-nitroanilide and was identified by PMF-MALDI-TOF MS. Asclepain f is the first peptidase cloned and expressed from mRNA isolated from plant la...

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Research paper thumbnail of Isolation and Characterization of Hieronymain II, Another Peptidase Isolated from Fruits of Bromelia hieronymi Mez (Bromeliaceae)

The Protein Journal, 2006

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Research paper thumbnail of Philibertain g I, the Most Basic Cysteine Endopeptidase Purified from the Latex of Philibertia gilliesii Hook. et Arn. (Apocynaceae)

The Protein Journal, 2005

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Research paper thumbnail of Granulosain I, a Cysteine Protease Isolated from Ripe Fruits of Solanum granuloso -leprosum (Solanaceae)

The Protein Journal, 2008

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Research paper thumbnail of Purificación de una nueva endopeptidasa aislada de frutos de Bromelia hieronymi Mez (Bromelia-ceae)

Acta Farmaceutica Bonaerense, 2002

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Research paper thumbnail of Proteases present in latex from fruits of maclura pomifera raf. schneid. moraceae

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Research paper thumbnail of Proteasas de plantas superiores ii. Ficina ( ec 3.4.22.32 )

Bookmarks Related papers MentionsView impact

Research paper thumbnail of Desarrollo de procesos destinados a minimizar el impacto ambiental de las curtiembres de la provincia de Buenos Aires

Bookmarks Related papers MentionsView impact

Research paper thumbnail of New purified plant proteinases for the food industry

Acta Alimentaria, 1991

A crude enzyme preparation obtained from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) s... more A crude enzyme preparation obtained from unripe fruits of Bromelia hieronymi Mez (Bromeliaceae) shows a broad pH range of optimum proteolytic activity and a good thermal stability up to 45°C. Diafiltration followed by ion-exchange chromatography allows the separation of four proteolytic components of closely related molecular weights

Bookmarks Related papers MentionsView impact

Research paper thumbnail of Proteasas de plantas superiores. I. Caracteristicas generales, rol fisiologico y aplicaciones

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Research paper thumbnail of Proteasas de plantas superiores

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Research paper thumbnail of Insights into the hydrolytic activity of Asclepias fruticosa L. protease

Biotechnology Letters, 2019

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Research paper thumbnail of Structural Properties of Macrodontain I, a Cysteine Protease from Pseudananas macrodontes (Morr.) Harms (Bromeliaceae)

Applied biochemistry and biotechnology, Jan 15, 2018

The primary structure of macrodontain I, a peptidase from Pseudananas macrodontes fruits, was det... more The primary structure of macrodontain I, a peptidase from Pseudananas macrodontes fruits, was determined using Edman's degradation. The enzyme is a non-glycosylated peptidase composed by 213 amino acids with a calculated molecular weight of 23,486.18 Da, pI value 6.99, and a molar extinction coefficient at 280 nm of 61,685 M cm. The alignment of the sequence of macrodontain I with those cysteine peptidases from species belonging to the family Bromeliaceae showed the highest identity degree (87.74%) against fruit bromelain. A remarkable fact is that all these peptidase sequences show two Met contiguous residues (Met121 and 122) and the nonapeptide VPQSIDWRD located in the mature N-terminal region. Residues Cys26 and His159, which constitute the catalytic dyad in all cysteine peptidases, as well as active site residues Gln20 and Asn176, characteristic of Clan C1A, are conserved in macrodontain I. The 3-D model suggests that the enzyme belongs to the α + β class of proteins, with t...

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

LWT - Food Science and Technology, 2012

... Maria Alicia Corrons , E-mail The Corresponding Author , Juan Ignacio Bertucci , E-mail The C... more ... Maria Alicia Corrons , E-mail The Corresponding Author , Juan Ignacio Bertucci , E-mail The Corresponding Author , Constanza Silvina Liggieri , E-mail The Corresponding Author , Laura María Isabel López , E-mail The Corresponding Author , Mariela Anahí Bruno ...

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Research paper thumbnail of Purification of a new endopeptidase isolated from fruits of Bromelia hieronymi Mez (Bromeliaceae)

Acta Farmacéutica …, 2002

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Research paper thumbnail of Proteolytic extracts of three Bromeliaceae species as eco-compatible tools for leather industry

Environmental science and pollution research international, Jan 2, 2018

Most tanneries use high proportions of Na2S and CaO during the dehairing step, resulting in efflu... more Most tanneries use high proportions of Na2S and CaO during the dehairing step, resulting in effluents of high alkalinity and large amounts of suspended solid, besides the risk of liberating the toxic H2S. Solid waste rich in protein is another environmental problem of tanneries. Enzymes are an interesting technological tool for industry due to their biodegradability, nontoxic nature, and nonpolluting effluent generation. In the leather industry, proteases have been chosen as a promising eco-friendly alternative to Na2S/CaO dehairing. Extracts with high proteolytic activity have been obtained from fruits of Bromeliaceae species: Bromelia balansae Mez (Bb), Bromelia hieronymi Mez (Bh), and Pseudananas macrodontes (Morr.) Harms (Pm). In this work, Bb, Bh, and Pm have been studied for application in the leather industry, focusing in their dehairing properties. Enzymatic activities were measured against collagen, keratin, elastin, and epidermis while a dehairing assay was performed by em...

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Research paper thumbnail of A Bowman-Birk protease inhibitor purified, cloned, sequenced and characterized from the seeds of Maclura pomifera (Raf.) Schneid

Planta, Jan 24, 2016

A new BBI-type protease inhibitor with remarkable structural characteristics was purified, cloned... more A new BBI-type protease inhibitor with remarkable structural characteristics was purified, cloned, and sequenced from seeds of Maclura pomifera , a dicotyledonous plant belonging to the Moraceae family. In this work, we report a Bowman-Birk inhibitor (BBI) isolated, purified, cloned, and characterized from Maclura pomifera seeds (MpBBI), the first of this type from a species belonging to Moraceae family. MpBBI was purified to homogeneity by RP-HPLC, total RNA was extracted from seeds of M. pomifera, and the 3'RACE-PCR method was applied to obtain the cDNA, which was cloned and sequenced. Peptide mass fingerprinting (PMF) analysis showed correspondence between the in silico-translated protein and MpBBI, confirming that it corresponds to a new plant protease inhibitor. The obtained cDNA encoded a polypeptide of 65 residues and possesses 10 cysteine residues, with molecular mass of 7379.27, pI 6.10, and extinction molar coefficient of 9105 M(-1) cm(-1). MpBBI inhibits strongly tryp...

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Research paper thumbnail of Purification and characterization of a new plant endopeptidase isolated from latex of Asclepias fruticosa L. (Asclepiadaceae)

Journal of protein chemistry, 2001

Asclepias fruticosa L. is a small shrub containing latex with proteolytic activity. The crude ext... more Asclepias fruticosa L. is a small shrub containing latex with proteolytic activity. The crude extract (latex diluted 1:250 and ultracentrifuged) contained 276 microg of protein/mL and the proteolytic activity reached 1.2 caseinolytic U/mL. This enzyme preparation was very stable even after 2 hours at 45 degrees C, but was quickly inactivated after 5 minutes at 80 degrees C. Chromatographic purification was achieved by FPLC using a cation exchanger (SP-Sepharose FF). Thus, a unique proteolitically active fraction could be isolated, being homogeneous by bidimensional electrophoresis and mass spectrometry (Mr = 23,652). The optimum pH range was achieved at 8.5-10.5. The enzyme activity was completely inhibited by specific cysteine peptidases inhibitors. Isoelectric focusing followed by zymogram showed the enzyme had a pI greater than 9.3. The N-terminus sequence (LPDSVDWREKGVVFPIRNQGK) shows a great deal of similarity to those of the other cysteine endopeptidases isolated from latices ...

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Research paper thumbnail of A Novel Trypsin and α-Chymotrypsin Inhibitor from Maclura pomifera Seeds

Letters in Drug Design & Discovery, 2010

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

Journal of protein chemistry, 2003

A new peptidase, named hieronymain I, was purified to homogeneity from unripe fruits of Bromelia ... more 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.

Bookmarks Related papers MentionsView impact

Research paper thumbnail of Sequencing and characterization of asclepain f: the first cysteine peptidase cDNA cloned and expressed from Asclepias fruticosa latex

Planta, 2009

Asclepain f is a papain-like protease previously isolated and characterized from latex of Asclepi... more Asclepain f is a papain-like protease previously isolated and characterized from latex of Asclepias fruticosa. This enzyme is a member of the C1 family of cysteine proteases that are synthesized as preproenzymes. The enzyme belongs to the alpha + beta class of proteins, with two disulfide bridges (Cys22-Cys63 and Cys56-Cys95) in the alpha domain, and another one (Cys150-Cys201) in the beta domain, as was determined by molecular modeling. A full-length 1,152 bp cDNA was cloned by RT-RACE-PCR from latex mRNA. The sequence was predicted as an open reading frame of 340 amino acid residues, of which 16 residues belong to the signal peptide, 113 to the propeptide and 211 to the mature enzyme. The full-length cDNA was ligated to pPICZalpha vector and expressed in Pichia pastoris. Recombinant asclepain f showed endopeptidase activity on pGlu-Phe-Leu-p-nitroanilide and was identified by PMF-MALDI-TOF MS. Asclepain f is the first peptidase cloned and expressed from mRNA isolated from plant la...

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Research paper thumbnail of Isolation and Characterization of Hieronymain II, Another Peptidase Isolated from Fruits of Bromelia hieronymi Mez (Bromeliaceae)

The Protein Journal, 2006

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Research paper thumbnail of Philibertain g I, the Most Basic Cysteine Endopeptidase Purified from the Latex of Philibertia gilliesii Hook. et Arn. (Apocynaceae)

The Protein Journal, 2005

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Research paper thumbnail of Granulosain I, a Cysteine Protease Isolated from Ripe Fruits of Solanum granuloso -leprosum (Solanaceae)

The Protein Journal, 2008

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