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Marcelo Cristianini - One of the best experts on this subject based on the ideXlab platform.
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influence of high pressure homogenization on commercial protease from rhizomucor miehei effects on proteolytic and Milk clotting activities
Lwt - Food Science and Technology, 2015Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:Abstract This work studied the influence of high pressure homogenization (HPH) on a commercial fungal protease. The enzyme solutions (2 and 20 g/100 mL) were processed up to 190 MPa and the proteolytic activity (PA), Milk-clotting activity (MCA) and the rheological behavior of the Milk coagulation phase were evaluated. The effects of multi-pass (three cycles) HPH at 25 and 190 MPa was evaluated for enzyme processed at concentration of 2 g/100 mL. No differences in PA and MCA were observed for the samples of 2 g/100 mL of enzyme concentration processed by HPH. On the other hand, increase in PA (∼3%) and MCA (∼10%) were observed for the enzymes processed at 190 MPa at high concentration, which consequent faster clotting and higher consistency of the Milk Gel. The multi-pass increased PA (≤6%) but did not alter MCA nor improved the Milk coagulation phase. The results highlight that the energy supplied from HPH to enzyme at low concentration is not enough to promote positive changes in the enzyme coagulant profile; however, the HPH of solution with high enzyme concentration showed a positive effect, indicating that the collisions between enzymes during the process was important to reach the observed changes.
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high pressure homogenization of porcine pepsin protease effects on enzyme activity stability Milk coagulation profile and Gel development
PLOS ONE, 2015Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:This study investigated the effect of high pressure homogenization (HPH) (up to 190 MPa) on porcine pepsin (proteolytic and Milk-clotting activities), and the consequences of using the processed enzyme in Milk coagulation and Gel formation (rheological profile, proteolysis, syneresis, and microstructure). Although the proteolytic activity (PA) was not altered immediately after the HPH process, it reduced during enzyme storage, with a 5% decrease after 60 days of storage for samples obtained with the enzyme processed at 50, 100 and 150 MPa. HPH increased the Milk-clotting activity (MCA) of the enzyme processed at 150 MPa, being 15% higher than the MCA of non-processed samples after 60 days of storage. The enzyme processed at 150 MPa produced faster aggregation and a more consistent Milk Gel (G’ value 92% higher after 90 minutes) when compared with the non-processed enzyme. In addition, the Gels produced with the enzyme processed at 150 MPa showed greater syneresis after 40 minutes of coagulation (forming a more compact protein network) and lower porosity (evidenced by confocal microscopy). These effects on the Milk Gel can be associated with the increment in MCA and reduction in PA caused by the effects of HPH on pepsin during storage. According to the results, HPH stands out as a process capable of changing the proteolytic characteristics of porcine pepsin, with improvements on the Milk coagulation step and Gel characteristics. Therefore, the porcine pepsin submitted to HPH process can be a suitable alternative for the production of cheese.
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proteolytic and Milk clotting activities of calf rennet processed by high pressure homogenization and the influence on the rheological behavior of the Milk coagulation process
Innovative Food Science and Emerging Technologies, 2014Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:Abstract This work studied the effects of high pressure homogenization (HPH) on the performance of a commercial calf rennet. The enzyme solution was processed at 50, 100, 150 and 190 MPa and then stored for up to five days at 4 °C. The effects were evaluated on the proteolytic and Milk-clotting activities of the enzyme and on the rheological behavior of the Milk Gels obtained using the processed enzyme. HPH caused a reduction in proteolytic activity with increase in pressure (up to 52% loss of activity at 190 MPa). At the first 48 h of storage, the processed enzyme maintained its activity while the non-processed sample showed a continuous reduction in activity. The results showed that HPH processing did not alter the Milk-clotting activity and the rheological tests showed high G' values for the Milk coagulated with the enzyme processed at 190 MPa (7% higher after 84 min of coagulation). Thus, HPH improves the Milk coagulation by calf rennet and reduces the proteolytic activity of enzyme, which may improve the quality of fresh cheeses, especially after their storage. Industrial relevance The changes caused by HPH in the calf rennet improved the cheese manufacturing process and the quality of the product (higher consistency of the Milk Gel and lower proteolysis during storage). Therefore, the HPH processing of calf rennet can improve its application in the dairy industry to obtain high quality fresh cheese and an extended shelf-life.
Bruno Ricardo De Castro Leite - One of the best experts on this subject based on the ideXlab platform.
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influence of high pressure homogenization on commercial protease from rhizomucor miehei effects on proteolytic and Milk clotting activities
Lwt - Food Science and Technology, 2015Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:Abstract This work studied the influence of high pressure homogenization (HPH) on a commercial fungal protease. The enzyme solutions (2 and 20 g/100 mL) were processed up to 190 MPa and the proteolytic activity (PA), Milk-clotting activity (MCA) and the rheological behavior of the Milk coagulation phase were evaluated. The effects of multi-pass (three cycles) HPH at 25 and 190 MPa was evaluated for enzyme processed at concentration of 2 g/100 mL. No differences in PA and MCA were observed for the samples of 2 g/100 mL of enzyme concentration processed by HPH. On the other hand, increase in PA (∼3%) and MCA (∼10%) were observed for the enzymes processed at 190 MPa at high concentration, which consequent faster clotting and higher consistency of the Milk Gel. The multi-pass increased PA (≤6%) but did not alter MCA nor improved the Milk coagulation phase. The results highlight that the energy supplied from HPH to enzyme at low concentration is not enough to promote positive changes in the enzyme coagulant profile; however, the HPH of solution with high enzyme concentration showed a positive effect, indicating that the collisions between enzymes during the process was important to reach the observed changes.
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high pressure homogenization of porcine pepsin protease effects on enzyme activity stability Milk coagulation profile and Gel development
PLOS ONE, 2015Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:This study investigated the effect of high pressure homogenization (HPH) (up to 190 MPa) on porcine pepsin (proteolytic and Milk-clotting activities), and the consequences of using the processed enzyme in Milk coagulation and Gel formation (rheological profile, proteolysis, syneresis, and microstructure). Although the proteolytic activity (PA) was not altered immediately after the HPH process, it reduced during enzyme storage, with a 5% decrease after 60 days of storage for samples obtained with the enzyme processed at 50, 100 and 150 MPa. HPH increased the Milk-clotting activity (MCA) of the enzyme processed at 150 MPa, being 15% higher than the MCA of non-processed samples after 60 days of storage. The enzyme processed at 150 MPa produced faster aggregation and a more consistent Milk Gel (G’ value 92% higher after 90 minutes) when compared with the non-processed enzyme. In addition, the Gels produced with the enzyme processed at 150 MPa showed greater syneresis after 40 minutes of coagulation (forming a more compact protein network) and lower porosity (evidenced by confocal microscopy). These effects on the Milk Gel can be associated with the increment in MCA and reduction in PA caused by the effects of HPH on pepsin during storage. According to the results, HPH stands out as a process capable of changing the proteolytic characteristics of porcine pepsin, with improvements on the Milk coagulation step and Gel characteristics. Therefore, the porcine pepsin submitted to HPH process can be a suitable alternative for the production of cheese.
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proteolytic and Milk clotting activities of calf rennet processed by high pressure homogenization and the influence on the rheological behavior of the Milk coagulation process
Innovative Food Science and Emerging Technologies, 2014Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:Abstract This work studied the effects of high pressure homogenization (HPH) on the performance of a commercial calf rennet. The enzyme solution was processed at 50, 100, 150 and 190 MPa and then stored for up to five days at 4 °C. The effects were evaluated on the proteolytic and Milk-clotting activities of the enzyme and on the rheological behavior of the Milk Gels obtained using the processed enzyme. HPH caused a reduction in proteolytic activity with increase in pressure (up to 52% loss of activity at 190 MPa). At the first 48 h of storage, the processed enzyme maintained its activity while the non-processed sample showed a continuous reduction in activity. The results showed that HPH processing did not alter the Milk-clotting activity and the rheological tests showed high G' values for the Milk coagulated with the enzyme processed at 190 MPa (7% higher after 84 min of coagulation). Thus, HPH improves the Milk coagulation by calf rennet and reduces the proteolytic activity of enzyme, which may improve the quality of fresh cheeses, especially after their storage. Industrial relevance The changes caused by HPH in the calf rennet improved the cheese manufacturing process and the quality of the product (higher consistency of the Milk Gel and lower proteolysis during storage). Therefore, the HPH processing of calf rennet can improve its application in the dairy industry to obtain high quality fresh cheese and an extended shelf-life.
Sylvie Marchesseau - One of the best experts on this subject based on the ideXlab platform.
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Effect of mono or co-culture of EPS-producing Streptococcus thermophilus strains on the formation of acid Milk Gel and the appearance of texture defects
International Dairy Journal, 2019Co-Authors: Thi Binh An Nguyen, Michael Nigen, Luciana Jimenez, Hassina Ait-abderahim, Laetitia Picart-palmade, Sylvie MarchesseauAbstract:One acidifying (ST1) and two texturing strains (ST2 and ST3) of Streptococcus thermophilus were used as pure or co-cultures to identify and understand their effects on the structuring of acid Milk Gels and on the appearance of texture defects, i.e., syneresis and graininess. Symbiosis between specific texturing and acidifying strains reduced acidification time and increased exocellular polysaccharide (EPS) content. The texturing strain could simultaneously produce low and high molar mass EPS and their distribution in mass and/or in number were influenced by the proportion of acidifying to texturing strain used. The results of this study suggest that the high molar mass EPS contributes to acid Gel firmness, but less so compared with the acidification rate. The ability of strain ST3 to prevent texture defects, specifically graininess, did not depend on the acidification kinetics or final EPS content, but rather on the structural properties of EPS and/or the bacterial chain morphology.
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A multi-scale approach to identify the role of heat treatment, Milk protein composition and starter culture on the Gel formation and the texture defects of acid Milk Gel
Food Hydrocolloids, 2018Co-Authors: An Thi-binh Nguyen, Sylvie Marchesseau, Michael Nigen, Luciana Jimenez, Hassina Ait-abderahim, Charles Cunault, Laetitia Picart-palmadeAbstract:Two exocellular polysaccharide (EPS)-producing starter cultures, named B and C, were used to investigate the effect of (1) heat treatment, (2) supplementation in whey protein (WP) and (3) presence of EPS on the Gel formation, Gel microstructure and occurrence of texture defect, i.e. spontaneous syneresis and graininess, of acid Milk Gel. In skim Milk (SM), culture B induced a slow acidification and produced a medium level of EPS (50 mg glucose kg−1). Heated at high temperature (95 °C, 6 min), the WP denaturation of the SM increased the syneresis of the Gel and generated grains. Culture C had faster acidification kinetics and produced a higher quantity of EPS (80 mg glucose kg−1) that contribute to generating higher intrinsic viscosity to acid Milk Gel compare to culture B. Neither syneresis nor grain was observed in high heated SM Gel obtained with culture C. The Milk Gel microstructure observed by confocal laser scanning microscopy showed that bacterial chains of culture B were short and embedded in the protein network while chains of culture C were longer, forming large clusters and mainly located in the Gel pores. The overall results suggested that the presence of denatured WP is a cause of grain formation but that the curled chains of culture C surrounded by EPS could induce a steric hindrance during the Gel structuring and prevent the growth of grain. The Milk enrichment in WP increased the firmness, the water-holding capacity of acid Gel but has generated graininess defect that could be reduced by the starter culture.
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acid Milk Gel formation as affected by total solids content
Journal of Food Science, 1997Co-Authors: E Gastaldi, A Lagaude, Sylvie Marchesseau, Tarodo B De La FuenteAbstract:Reconstituted skim Milk with varying concentrations of total solids was coagulated using glucono-δ-lactone (GDL). Microscopic, turbidimetric and rheological procedures were used to examine mineral solubilization, buffering capacity, casein dissociation and micellar solvation during Gelation. Total solids of the Milk affected pH of the onset of Gelation attributable to differences in colloidal calcium phosphate in the casein particles during acidification. Firmness and elasticity of the resulting Gel increased with total solids from a more direct contribution of dry matter during the last stage of acid Milk Gel formation.
Stephanie Weidmann - One of the best experts on this subject based on the ideXlab platform.
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Exopolysaccharide produced by Weissella confusa: Chemical characterisation, rheology and bioactivity
International Dairy Journal, 2019Co-Authors: Insaf Samira Benhouna, Arnaud Heumann, Aurélie Rieu, Jean Guzzo, Mabrouk Kihal, Guessas Bettache, Dominique Champion, Christian Coelho, Stephanie WeidmannAbstract:The purpose of this study was to characterise the production of exopolysaccharide (EPS) by indigenous lactic acid bacteria (LAB) isolated from traditional Algerian dairy products and to evaluate their possible use in agri-foods. Among the collection of isolated strains, the strain Weissella confusa (W4) was selected for its ability to produce EPS once exposed to a sucrose culture medium. EPS produced were first isolated with a standardised method and further characterised in terms of molecular size, antioxidant activity, and rheological properties. Its direct implication in the texture and syneresis of acid Milk Gel was evaluated offering interesting industrial applications for its use during processes dealing with dairy products.
Alline Artigiani Lima Tribst - One of the best experts on this subject based on the ideXlab platform.
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influence of high pressure homogenization on commercial protease from rhizomucor miehei effects on proteolytic and Milk clotting activities
Lwt - Food Science and Technology, 2015Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:Abstract This work studied the influence of high pressure homogenization (HPH) on a commercial fungal protease. The enzyme solutions (2 and 20 g/100 mL) were processed up to 190 MPa and the proteolytic activity (PA), Milk-clotting activity (MCA) and the rheological behavior of the Milk coagulation phase were evaluated. The effects of multi-pass (three cycles) HPH at 25 and 190 MPa was evaluated for enzyme processed at concentration of 2 g/100 mL. No differences in PA and MCA were observed for the samples of 2 g/100 mL of enzyme concentration processed by HPH. On the other hand, increase in PA (∼3%) and MCA (∼10%) were observed for the enzymes processed at 190 MPa at high concentration, which consequent faster clotting and higher consistency of the Milk Gel. The multi-pass increased PA (≤6%) but did not alter MCA nor improved the Milk coagulation phase. The results highlight that the energy supplied from HPH to enzyme at low concentration is not enough to promote positive changes in the enzyme coagulant profile; however, the HPH of solution with high enzyme concentration showed a positive effect, indicating that the collisions between enzymes during the process was important to reach the observed changes.
-
high pressure homogenization of porcine pepsin protease effects on enzyme activity stability Milk coagulation profile and Gel development
PLOS ONE, 2015Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:This study investigated the effect of high pressure homogenization (HPH) (up to 190 MPa) on porcine pepsin (proteolytic and Milk-clotting activities), and the consequences of using the processed enzyme in Milk coagulation and Gel formation (rheological profile, proteolysis, syneresis, and microstructure). Although the proteolytic activity (PA) was not altered immediately after the HPH process, it reduced during enzyme storage, with a 5% decrease after 60 days of storage for samples obtained with the enzyme processed at 50, 100 and 150 MPa. HPH increased the Milk-clotting activity (MCA) of the enzyme processed at 150 MPa, being 15% higher than the MCA of non-processed samples after 60 days of storage. The enzyme processed at 150 MPa produced faster aggregation and a more consistent Milk Gel (G’ value 92% higher after 90 minutes) when compared with the non-processed enzyme. In addition, the Gels produced with the enzyme processed at 150 MPa showed greater syneresis after 40 minutes of coagulation (forming a more compact protein network) and lower porosity (evidenced by confocal microscopy). These effects on the Milk Gel can be associated with the increment in MCA and reduction in PA caused by the effects of HPH on pepsin during storage. According to the results, HPH stands out as a process capable of changing the proteolytic characteristics of porcine pepsin, with improvements on the Milk coagulation step and Gel characteristics. Therefore, the porcine pepsin submitted to HPH process can be a suitable alternative for the production of cheese.
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proteolytic and Milk clotting activities of calf rennet processed by high pressure homogenization and the influence on the rheological behavior of the Milk coagulation process
Innovative Food Science and Emerging Technologies, 2014Co-Authors: Bruno Ricardo De Castro Leite, Alline Artigiani Lima Tribst, Marcelo CristianiniAbstract:Abstract This work studied the effects of high pressure homogenization (HPH) on the performance of a commercial calf rennet. The enzyme solution was processed at 50, 100, 150 and 190 MPa and then stored for up to five days at 4 °C. The effects were evaluated on the proteolytic and Milk-clotting activities of the enzyme and on the rheological behavior of the Milk Gels obtained using the processed enzyme. HPH caused a reduction in proteolytic activity with increase in pressure (up to 52% loss of activity at 190 MPa). At the first 48 h of storage, the processed enzyme maintained its activity while the non-processed sample showed a continuous reduction in activity. The results showed that HPH processing did not alter the Milk-clotting activity and the rheological tests showed high G' values for the Milk coagulated with the enzyme processed at 190 MPa (7% higher after 84 min of coagulation). Thus, HPH improves the Milk coagulation by calf rennet and reduces the proteolytic activity of enzyme, which may improve the quality of fresh cheeses, especially after their storage. Industrial relevance The changes caused by HPH in the calf rennet improved the cheese manufacturing process and the quality of the product (higher consistency of the Milk Gel and lower proteolysis during storage). Therefore, the HPH processing of calf rennet can improve its application in the dairy industry to obtain high quality fresh cheese and an extended shelf-life.