@article {Schaffer:May 2001:1418-2874:671,
	author = "Schaffer, B.",
	author = "Szakaly, S.",
	author = "Lorinczy, D.",
	title = "Processed Cheeses Made With and Without Peptization: Submicroscopic structure and thermodynamic characteristics",
	journal = "Journal of Thermal Analysis and Calorimetry",
	volume = "64",
	year = "May 2001",
	abstract = "The osteoporosis is regarded as a widespread disease all over the world. In the prevention therapy of this disease there is a primary role of the daily calcium intake with the proper Ca:P ratio (1:1&#8211;1:2). The primary source of Ca for people the dairy products are implied, from which only the processed cheeses have inadequate ratio of Ca:P. In cheeses processed without peptization developed in the Hungarian Dairy Research Institute (HDRI) the Ca:P ratio meets the requirements (1.5:1), moreover these products can be enriched with Ca.<P></P>In this study we used both processing technologies. The electronmicroscopic photographs demonstrate the differences clearly. The traditionally processed cheese (with peptization) has a `spongy' structure well known from literature, while a space-net can be seen resulting from the casein-filamentous hydrocolloid interaction in the structure of heat-treated cheese without peptization. DSC curves are the same in the temperature range 0&#8211;40&#176;C, showing endotherm melting process in two well-distinguished temperature interval (0&#8211;20 and 22&#8211;40&#176;C). They are different in the temperature interval 40&#8211;100&#176;C: in the case of processed cheese with peptization the gel-sol transformation gives a higher endotherm peak in a narrow temperature range, while for heat-treated cheese without peptization this temperature range is wider with a lower endotherm peak.<P></P>Both electronmicroscopic and DSC investigations have proved that contrary to the traditionally processed cheese where the structure is formed by the linked peptized protein, in the heat- processed cheese without peptization the frame-forming element is the huge hydrocolloid molecule interacted with the protein. The enthalpy change is substantially lower at the disintegration of the latter structure.",
	pages = "671-679(9)",
	url = "http://www.ingentaconnect.com/content/klu/jtan/2001/00000064/00000002/00353553"
	doi = "doi:10.1023/A:1011532009021"
}