http://www.similacalimentumhesaplama.com/assets/files/Fiocchi_A_WAO_DRACMA_guidelines_2010_ISPA_c_sayfa_9_57_58.pdf

World Allergy Organization (WAO) Diagnosis and Rationale for Action against Cow's Milk Allergy (DRACMA) Guidelines

Alessandro Fiocchi, MD, Pediatric Division, Department of Child and Maternal Medicine, University of Milan Medical School at the Melloni Hospital, Milan 20129, Italy. Holger Schünemann, MD, Department of Clinical Epidemiology & Biostatistics, McMaster University Health Sciences Centre, 1200 Main Street West Hamilton, ON L8N 3Z5, Canada. Sami L. Bahna, MD, Pediatrics & Medicine, Allergy & Immunology, Louisiana State University Health Sciences Center, Shreveport, LA 71130. Andrea Von Berg, MD, Research Institute, Children s department , Marien-Hospital, Wesel, Germany. Kirsten Beyer, MD, Charité Klinik für Pädiatrie m.S. Pneumologie und Immunologie, Augustenburger Platz 1, D-13353 Berlin, Germany. Martin Bozzola, MD, Department of Pediatrics, British Hospital-Perdriel 74-CABA-Buenos Aires, Argentina. Julia Bradsher, PhD, Food Allergy & Anaphylaxis Network, 11781 Lee Jackson Highway, Suite 160, Fairfax, VA 22033. Jan Brozek, MD, Department of Clinical Epidemiology & Biostatistics, McMaster University Health Sciences Centre, 1200 Main Street West Hamilton, ON L8N 3Z5, Canada. Enrico Compalati, MD, Allergy & Respiratory Diseases Clinic, Department of Internal Medicine. University of Genoa, 16132, Genoa, Italy. Motohiro Ebisawa, MD, Department of Allergy, Clinical Research Center for Allergy and Rheumatology, Sagamihara National Hospital, Kanagawa 228-8522, Japan. Maria Antonieta Guzman, MD, Immunology and Allergy Division, Clinical Hospital University of Chile, Santiago, Chile. Santos Dumont 999. Haiqi Li, MD, Professor of Pediatric Division, Department of Primary Child Care, Children’s Hospital, Chongqing Medical University, China, 400014. Ralf G. Heine, MD, FRACP, Department of Allergy & Immunology, Royal Children’s Hospital, University of Melbourne, Murdoch Children’s Research Institute, Melbourne, Australia. Paul Keith, MD, Allergy and Clinical Immunology Division, Department of Medicine, McMaster University, Hamilton, Ontario, Canada. Gideon Lack, MD, King’s College London, Asthma-UK Centre in Allergic Mechanisms of Asthma, Department of Pediatric Allergy, St Thomas’ Hospital, London SE1 7EH, United Kingdom. Massimo Landi, MD, National Pediatric Healthcare System, Italian Federation of Pediatric Medicine, Territorial Pediatric Primary Care Group, Turin, Italy. Alberto Martelli, MD, Pediatric Division, Department of Child and Maternal Medicine, University of Milan Medical School at the Melloni Hospital, Milan 20129, Italy. Fabienne Rancé, MD, Allergologie, Hôpital des Enfants, Pôle Médicochirurgical de Pédiatrie, 330 av. de Grande Bretagne, TSA 70034, 31059 Toulouse CEDEX, France. Hugh Sampson, MD, Jaffe Food Allergy Institute, Mount Sinai School of Medicine, One Gustave L. Levy Place, NY 10029-6574. Airton Stein, MD, Conceicao Hospital, Porto Alegre, Brazil. Luigi Terracciano, MD, Pediatric Division, Department of Child and Maternal Medicine, University of Milan Medical School at the Melloni Hospital, Milan 20129, Italy. Stefan Vieths, MD, Division of Allergology, Paul-EhrlichInstitut, Federal Institute for Vaccines and Biomedicines, Paul-Ehrlich-Str. 51-59, D-63225 Langen, Germany.

World Allergy Organization (WAO) Diagnosis and Rationale for Action against Cow's Milk Allergy (DRACMA) Guidelines.

This review intended to give a brief idea of the importance of proteases applications. Processes that involve protein hydrolysis steps find wide ranging utilizations, such as cleaning process, proteomic studies, or food biotechnology process. Many positive effects hoped for with food processing can be achieved by protein hydrolysis using specific proteases, changing nutritional, bioactive and functional properties of food proteins, which include improved digestibility, modifications of sensory quality (such as texture or taste), improvement of antioxidant capability or reduction in allergenic compounds. Protease applications in industrial processes are constantly being introduced and can be advantageous compared to chemical processes, by increasing hydrolysis specificity, product preservation and purity, and reducing environmental impact. Differences in specificity between proteases are very important to take in to consideration as a guide for the choice of protease according to the protein source to be hydrolyzed or predicted products. In this present review, some aspects of the processes that involve protein hydrolysis steps are discussed, especially considering the application of specific proteases as a tool on food biotechnology.

Protein hydrolysis using proteases: An important tool for food biotechnology

Recent advances in exploiting goat's milk: Quality, safety and production aspects

http://ssu.ac.ir/cms/fileadmin/user_upload/Mtahghighat/tfood/ARTICLES/milk/Compositional__technological_and_nutritional_aspects_of_dromedary_camel_milk.pdf

Compositional, technological and nutritional aspects of dromedary camel milk

http://camelnet.eu/wp-content/uploads/2014/09/thechallengeofcowmilkproteinallergy.pdf

The challenge of cow milk protein allergy

Are camel milk proteins convenient to the nutrition of cow milk allergic children

Chlorpyrifos induced reproductive toxicity in male mice

Bioactive Components in Camel Milk

Camel calf rennet (CCR) and buffalo calf rennet (BCR) were prepared from dried abomasa to study their physicochemical properties and electrophoretic behaviour and to carry out an immunological characterization of the rennet proteins. CCR was more thermostable than BCR. The milk clotting activity of both rennets increased as pH decreased. The optimum temperatures for CCR and BCR were 50 and 45 degrees C respectively. CCR was more sensitive to increased CaCl2 in milk than BCR. Addition of NaCl to milk in the range 0-100 g/l resulted in a marked decrease in the clotting activity of both rennets. When the rennets were treated with acetone, the activity of BCR was completely destroyed, but that of CCR was unaffected. The proteolytic activity of CCR was higher than that of BCR and pepsin towards both camel and cows' milk caseins at pH 6.0. SDS-PAGE electrophoretic patterns of CCR and BCR proteins gave two major bands with molecular masses estimated as 52 and 39 kDa for CCR and 50 and 35 kDa for BCR. Immunodiffusion and immunoelectrophoresis using anti-CCR serum demonstrated immunological cross reactivity between CCR and BCR.

Elsayed I. El-Agamy

Papers

The challenge of cow milk protein allergy

Are camel milk proteins convenient to the nutrition of cow milk allergic children

Chlorpyrifos induced reproductive toxicity in male mice

Bioactive Components in Camel Milk

Physicochemical, molecular and immunological characterization of camel calf rennet: a comparison with buffalo rennet