Characterization of rennet-induced gels using calf rennet processed by high pressure homogenization: Effects on proteolysis, whey separation, rheological properties and microstructure

Leite, Bruno Ricardo de Castro; Tribst, Alline Artigiani Lima; Oliveira, Mauro; Cristianini, Nello

doi:10.1016/j.ifset.2014.05.007

Cited by 11 publications

(13 citation statements)

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“…A volume of 1 L of the commercial porcine pepsin solution prepared at 0.1% (w/v) in 0.2M sodium acetate buffer (pH 5.6) was homogenized at 150 MPa using an inlet temperature of 23°C. Samples (200 mL) were collected and cooled to 23°C and a non-processed sample of porcine pepsin protease evaluated as the control sample [ 23 ].…”

Section: Methodsmentioning

confidence: 99%

“…The mixture was then pre-incubated at 35°C/ 10 minutes, and subsequently 360 μL of enzyme solution (0.1%, w/v) were added and the time count started. After 40 min, 3 h, 6 h, 18 h and 24 h of coagulation at 35°C, 20 mg samples were collected and prepared for Capillary zone electrophoresis (CZE) following the method described in [ 23 ]. Capillary zone electrophoresis (CZE) was then carried out using the methodology described in [ 23 ].…”

Section: Methodsmentioning

confidence: 99%

“…After 40 min, 3 h, 6 h, 18 h and 24 h of coagulation at 35°C, 20 mg samples were collected and prepared for Capillary zone electrophoresis (CZE) following the method described in [ 23 ]. Capillary zone electrophoresis (CZE) was then carried out using the methodology described in [ 23 ]. The capillary electropherogram separation of a 1:1:1 mixture of α s -CN, β-CN and κ-CN and identification of the major caseins by analysis of the casein standards are presented in [ 23 ].…”

Section: Methodsmentioning

confidence: 99%

“…Capillary zone electrophoresis (CZE) was then carried out using the methodology described in [ 23 ]. The capillary electropherogram separation of a 1:1:1 mixture of α s -CN, β-CN and κ-CN and identification of the major caseins by analysis of the casein standards are presented in [ 23 ].…”

Section: Methodsmentioning

confidence: 99%

“…The effects of HPH were dependent on the level of pressure homogenization applied, the temperature of the enzyme during the process, the nature of the enzyme studied and the pH of homogenization [ 19 , 20 , 21 ]. Specifically for milk coagulants, HPH was able to reduce the unspecific proteolytic activity of calf rennet, increase its specificity in the milk-clotting formation, improve enzyme stability with time and improve the characteristics of the milk gel produced [ 22 , 23 ].…”

Section: Introductionmentioning

confidence: 99%

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High Pressure Homogenization of Porcine Pepsin Protease: Effects on Enzyme Activity, Stability, Milk Coagulation Profile and Gel Development

2015

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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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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%