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The Development Of Alkaline Phosphatase Based Paper Bioreporter For Evaluation Of Milk Pasteurization

Alkaline phosphatase (ALP) is a natural milk enzyme. It has been used as
reporter for process controls in food industry. Since ALP denatures at
pasteurization temperature (at 63&deg / C or 72&deg / ) its detection in milk confirms the
unproper pasteurization. There are different detection procedures such as
colorimetric, fluorometric methods and immunoassays for ALP in milk.
However, they are time consuming processes and require specific instruments
and qualified staff. In this study, new, semiquantitative, disposable, cheap and
practical paper bioreporter have been developed for ALP detection.
In optimization studies, 1mg/mL p-NPP in 0.1 M glycine buffer at pH 9.5 and 0.5
mg/mL bromocresol green in 1.0 M Tris-HCl buffer at pH 9.5 were determined
as optimum for ALP bioreporter as a result of visual inspection and green color
intensity analyses.The effects of samples temperature and pH of on the response of bioreporter
were tested. Milk samples at pH 5.0, 5.5, 6.0 and 6.5 and milks stored at 37&deg / C,
room temperature and 4&deg / C did not affect the response of bioreporter.
Also the response of bioreporter against milk samples from different animals
(cattle, sheep and goat) and cow&rsquo / s milk from different location in Turkey were
evaluated. The appropriate responses were observed by bioreporter.
Whatman filter papers, cotton and bandage were used as support materials to
construct bioreporter and Whatman filter papers were selected as the most
applicaple support material.
Finally, stability tests were carried out at 4&deg / C and room temperature and 40
days at 4&deg / C was determined as shelf life of bioreporter.

Identiferoai:union.ndltd.org:METU/oai:etd.lib.metu.edu.tr:http://etd.lib.metu.edu.tr/upload/3/12610674/index.pdf
Date01 June 2009
CreatorsKarakas, Ceren
ContributorsOktem, Huseyin Avni
PublisherMETU
Source SetsMiddle East Technical Univ.
LanguageEnglish
Detected LanguageEnglish
TypeM.S. Thesis
Formattext/pdf
RightsTo liberate the content for public access

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