2000
DOI: 10.1016/s0308-8146(00)00065-0
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Effect of heat treatment on the rennet clotting time of goat and cow milk

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Cited by 20 publications
(20 citation statements)
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“…12% (w/v) RM was prepared with milli-Q water (Millipore Corporation, Billerica, MA), and agitated (400 rpm) using a stirrer (JJ-1, Guohua Inc., Jiangshu, China) for 30 min at the ambient temperature (20 Ϯ 1C). The FM and RM were heated as described by Alloggio et al (2000) with some modification. One hundred fifty milliliters of each milk sample was added to sterile flask, hermetically sealed.…”
Section: Heat Treatmentsmentioning
confidence: 99%
“…12% (w/v) RM was prepared with milli-Q water (Millipore Corporation, Billerica, MA), and agitated (400 rpm) using a stirrer (JJ-1, Guohua Inc., Jiangshu, China) for 30 min at the ambient temperature (20 Ϯ 1C). The FM and RM were heated as described by Alloggio et al (2000) with some modification. One hundred fifty milliliters of each milk sample was added to sterile flask, hermetically sealed.…”
Section: Heat Treatmentsmentioning
confidence: 99%
“…Goat milk also contains higher proportion of fatty acids such as caproic, caprylic and capric, which are partly responsible for the unique flavor of fresh goat milk and its products [1]. In addition, the clotting behavior of goat milk was also different from cow milk [2]. In term of causing allergy, goat milk has been reported to have less allergenicity than cow milk [3].…”
Section: Introductionmentioning
confidence: 99%
“…The heat treatment applied to milk involves change in its physical and chemical properties such as whey protein, denaturation, and subsequent complex formation with j-casein and decrease in the soluble calcium amount (Allogio, Caponio, Pasqualone, & Gomes, 2000;Candioti, Meinardi, & Zalazar, 2004;Macej, Jovanovic, & Denin Djurdjevic, 2002;Singh & Waungana, 2001;Vasbinder, Rollema, & de Kruif, 2003). The interaction involves thiol-disulphide bond interchange reactions between the free thiol-disulphide and the denatured whey proteins, especially blactoglobulin and disulphide bond of j-casein (Anema, Lee, & Klostermeyer, 2007).…”
Section: Introductionmentioning
confidence: 99%