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Sequential and competitive adsorption of BSA and ��-lactoglobulin, and their resistance to exchange with [sigma]-lactalbumin and ��-caseinNasir, Adil 05 July 1995 (has links)
Graduation date: 1996
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Antimicrobial Activity of Casein Hydrolysates against Listeria monocytogenes and Escherichia coli O157:H7Christman, Jessica M 01 December 2010 (has links)
Listeriosis has the highest fatality and hospitalization rate among foodborne illnesses. Listeria monocytogenes causes listeriosis and is a difficult bacterium for ready-to-eat food processors to eliminate because of its ability to grow in the absence of oxygen and under refrigeration. Recently, milk and its proteins have gained recognition as the largest source of biologically active peptides, and, it stands reason that several antimicrobial peptides (AMP) can be released from casein as it is the most abundant milk protein. AMPs are commonly obtained by cutting the whole protein into peptide fragments using enzymes or by acidification. The objective of this study was to predict potential AMPs through computer aided tools, improve hydrolysate preparation, and determine trypsin and pepsin-casein hydrolysate antimicrobial activity in growth media and on frankfurters against two strains of Listeria monocytogenes (Scott A and 310) and Escherichia coli O157:H7 (Salami strain).
The prediction study procedure was to identify the most common variants of primary peptide sequences. The sequences were analyzed for greatest possible enzyme cuts on the protein, peptide masses, isoelectric point, net charge and percent hydrophilic residues using online proteomics programs. The fragments were explored for AMP commonalities: fragment length of 3 to 50 amino acids, positive (cationic) net charge, and hydrophilic residues between 25 and 50%. This technique identified 16 potential AMPs which proved that it is possible to screen for AMPs.
The method used to determine the trypsin-casein hydrolysate (TCH) and pepsin-casein hydrolysate (PCH) antimicrobial activity was to hydrolyze sodium caseinate with pepsin or trypsin. L. monocytogenes (strains Scott A and 310) were incubated in 0, 10, 20, and 40% PCH and 0 and 50% TCH concentrations over a 24 hour period. PCH suppressed growth of L. monocytogenes Scott A by 1.76 log CFU/mL and reduced initial populations of L. monocytogenes 310 and E. coli O157:H7 by 0.52 and 0.62 log CFU/ml, respectively. TCH had little or no effect on growth suppression of any of the three test organisms.
The frankfurter study was conducted by spot inoculating frankfurters with L. monocytogenes Scott A and then dipping frankfurters into one of five treatments (deionized water, pH 2.7 buffer, pH 5.1 buffer, pH 2.7 PCH, and pH 5.1 PCH) for 30 seconds; inoculated frankfurters that were not dipped served as controls. Frankfurters were incubated at 32°C for seven days. The results showed that there was no significant difference (p>0.05) in antimicrobial effectiveness among the treatments and control.
This study demonstrated that enzymatically derived casein hydrolysates somewhat inhibit growth of L. monocytogenes and E. coli O157:H7 in culture media, but were ineffective when applied to frankfurters. Casein hydrolysate solutions can be easily made in a processing facility for application in fluid systems such as an antimicrobial spray on beef carcasses and in milk, juice, sports drinks, soda, soups, and yogurt. It also could be used in solid systems such as frankfurters, cheese, ground beef, and processed or RTE foods.
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Gluten-free and casein-free diets as a form of alternative treatment for autism spectrum disordersWashnieski, Gwenda. January 2009 (has links) (PDF)
Thesis PlanA (M.S.)--University of Wisconsin--Stout, 2009. / Includes bibliographical references.
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Remineralization of initial carious lesions using CPP-ACP reagents in vitroGopalakrishnan, Vaishnavi Lekshmi. January 2010 (has links)
published_or_final_version / Paediatric Dentistry / Master / Master of Dental Surgery
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Remineralizing action of CPP-ACP reagents on artificial carious lesionsBuckshey, Sakshi. January 2011 (has links)
published_or_final_version / Paediatric Dentistry / Master / Master of Dental Surgery
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Colloidal Behaviour of Casein Micelles with ConcentrationKrishnankutty Nair, Pulari 14 September 2012 (has links)
Structure function changes of casein micelles were studied as a function of concentration using a non invasive concentration method, osmotic stressing. A combination of serum analysis, light scattering and rheological measurements were used to characterize the physico-chemical properties of casein micelles. In heated and unheated milk, rheological studies indicated that casein micelles behave as hard spheres of similar volume fractions, if the viscosity changes in the serum phase and the particle particle interactions are taken into account. The differences in the distribution of the heat induced complexes between colloidal and soluble phase affected the colloidal properties of casein micelles. Above 70 g L-1 protein, the protein particles were no longer free diffusing. Re-dilution of the suspensions showed no irreversible aggregation. The data suggested that in the range of concentration studied casein micelles behave as hard spheres. Age gelation was also investigated on heated and unheated concentrated milk. In unheated concentrated milk proteolysis played an important role in imparting an increase in viscosity by causing aggregation of the casein micelles. On the other hand, in heated milk, there was a significant effect of the whey protein aggregates, which increased their interaction with the casein micelles over time. This effect, together with proteolysis caused age gelation in heated concentrated milk. The method of concentration used in this research, osmotic stressing, was then compared to ultrafiltration. It was demostrated that these two methods are not equivalent, as shear and mixing during ultrafiltration cause rearrangements to the casein micells. The differences were clearly demonstrated by adding soluble caseins to the milk before or after concentration. This project brings a better understanding on the effects of concentration on the structure-function of casein micelles and the interactions occurring in milk proteins during concentration.
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Caseinomacropeptide - fractionation by means of membrane techniques and technological characterization /Thomä-Worringer, Corinna. January 2007 (has links)
Techn. University, Diss.--München.
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Coagulation properties of milk : association with milk protein composition and genetic polymorphism /Hallén, Elin, January 2008 (has links) (PDF)
Diss. (sammanfattning) Uppsala : Sveriges lantbruksuniv., 2008. / Härtill 5 uppsatser.
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Regulatory mechanisms of eukaryotic translation terminationKallmeyer, Adam K. January 2007 (has links) (PDF)
Thesis (Ph.D.)--University of Alabama at Birmingham, 2007. / Title from first page of PDF file (viewed on June 25, 2009). Includes bibliographical references.
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Hydrolasen in der Lebensmittelindustrie Regeneration von Filterstoffen und Herstellung funktioneller PeptideSchopp, Silke January 2008 (has links)
Zugl.: Hohenheim, Univ., Diss., 2008
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