• Food Science of Animal Resources
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• v.37 no.5
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• pp.743-751
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• 2017

During slaughtering, animal blood is typically discarded, resulting in water pollution. However, this discarded blood has valuable components, such as immunoglobulin (Ig). Although several studies have been conducted to develop methods for effective recycling of slaughterhouse blood, they have not been commercially utilized in Korea. Here, we extracted an Ig-rich fraction from porcine blood that was then subjected to various in vitro tests, including pathogen growth inhibition, antigenic cross-reactivity, and anti-toxin activity. The porcine immunoglobulin concentrate (PIC) was effectively purified by eliminating other components, such as albumin, and consisted of approximately $63.2{\pm}2.9%$ IgG and $7.2{\pm}0.4%$ IgM on a protein basis. The results showed that it significantly suppressed the growth of pathogenic bacteria, and bound to all tested pathogens, including both gram-positive and gram-negative species, although the degree of activity differed according to strain. The PIC bound to two types of lipopolysaccharide (LPS) obtained from Escherichia coli O111:B4 and Salmonella enterica serotype typhimurium in a concentration-dependent manner. In addition, the PIC restored the proliferation activity of the lymphoblast K-562 cells when co-incubated with pathogenic LPS. These results confirm that the PIC prepared in this study is a potentially valuable functional food material or diet supplement as an alternative to antibiotics that can protect animals from pathogenic bacteria.

• Korean Journal of Food Science and Technology
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• v.30 no.4
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• pp.988-991
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• 1998

Plasma proteins were obtained from bloods of slaughtered bovine and porcine and analyzed by Fast Protein Liquid Chromatography (FPLC). Serum albumin content decreased in the following order: Porcine Plasma Protein (PPP)> Bovine Plasma Protein (BPP)> Whey Protein Concentrate (WPC). Protein contents of BPP, PPP, and WPC determined by Kjeldahl method were 85.79%, 82.30%, and 84.38%, respectively. Compared to WPC, plasma proteins had higher emulsifying activity index (EAI) below 2% protein concentration and slightly lower EAI above 4% protein concentration. Plasma proteins had higher EAI in the acidic pH range and more dependence on NaCl than WPC. Also, EAI of plasma proteins with NaCl was higher in the acidic range than that of WPC. These results indicated that plasma protein can be utilized as a raw material for emulsifier.