Papers by Keyword: Porcine Blood

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Abstract: Livestock blood is a slaughtering by-product that has potential for animal protein sources, human consumption is limited due to its brown color causing dark hues to food and feed products. The aim of this work is to extract white and palatable protein from red cells of porcine blood. Red cells are hydrolyzed with papain and acidized with Hydrochloric acid, freed heme group is flocculated with Sodium Carboxy Methyl Cellulose (CMC) and separated by centrifugation, supernatant is the decoloring protein solution. The enzyme hydrolysis conditions and flocculation conditions are optimized. The optimal enzyme hydrolysis parameters are substrate concentration 6%, papain dosage 6000u/g, time 8h and pH 7.0. The optimal enzyme flocculation parameters are CMC dosage 0.8g/g, pH 2.7 and time 10min. Decoloring protein powder obtained by isoelectric precipitation, centrifugation and vacuum freeze-drying is 95% protein, only 1% ash, light-colored and almost tasteless.
3980
Abstract: An anaerobic solid state fermentation (ASSF) of porcine blood by two ferment agents was investigated. The free amino acids (FAA) content was applied as reference indicator, response surface design of Box-Behnken (BBD) was used to select the optimum conditions of ASSF of porcine blood. The optimum conditions were determined as porcine blood moisture of 76.0%, fermentation time of 7d, fermentation temperature of 39.0±0.5 oC, addition of the components of the mixture as follows: wheat bran 10.8 g , corn flour 1.2 g, Active 99 ferment agent I 0.768 g, Active 99 ferment agent II 0.19 g, porcine blood 86.0 g, resulting in FAA content of 23.8 mg/g. Evaluation experiments revealed that FAA content of 22.9 mg/g, which was 96.2% of the predicted value using Eq.2, and achieved a 14-fold increase comparing with the 1.5 mg/g which is the FAA content of unfermented mixture. It was confirmed that the protein of porcine blood was degraded into small peptides by Sodium dodecyl sulfate - polyacrylamide gel electrophoresis (SDS-PAGE).
2060
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