Bovine Blood Plasma (bovine + blood_plasma)

Distribution by Scientific Domains


Selected Abstracts


Preparation and Characterization of Hydrolyzed Proteins from Defibrinated Bovine Plasma

JOURNAL OF FOOD SCIENCE, Issue 2 2002
P.K.J.P.D. Wanasundara
ABSTRACT: Proteins from defibrinated bovine blood plasma were enzymatically hydrolyzed with food-grade microbial proteases Alcalase 2.4 L® and Flavourzyme L&TM;, and a substrate consisting of small peptides and free amino acids was obtained. Hydrolysis of the plasma proteins with Flavourzyme resulted in a maximum degree of hydrolysis of 43% at an enzyme concentration of 110 LAPU/g protein after 15.5 h of hydrolysis. Among the free amino acids in the hydrolysate, hydrophobic amino acids were predominant. The major plasma proteins were degraded due to hydrolysis; peptides of less than 1.04 kDa were dominant in the product when a high degree of hydrolysis was employed. [source]


Development and validation of an HPLC method for the determination of seven penicillin antibiotics in veterinary drugs and bovine blood plasma

JOURNAL OF SEPARATION SCIENCE, JSS, Issue 9 2009
Victoria F. Samanidou
Abstract Herein a quantitative method for the determination of seven penicillins in bovine plasma and veterinary drugs has been developed. Amoxicillin (AMO), ampicillin (AMP), penicillin G (PENG), penicillin V (PENV), oxacillin (OXA), cloxacillin (CLO) and dicloxacillin (DICLO) were separated on a Perfectsil ODS-2 (250×4 mm, 5 ,m) column, using gradient elution, with a mobile phase of 0.1% v/v TFA and ACN,methanol (90:10 v/v). PDA detection was used at 240 nm. Penicillins were isolated from bovine plasma by SPE on Lichrolut RP-18 cartridges with mean recoveries from 85.7 to 113.5%. Colchicine (3 ng/,L) was used as an internal standard. The developed method was validated in terms of selectivity, linearity, accuracy, precision, stability and sensitivity. Repeatability (n = 5) and between-day precision (n = 5) revealed RSD < 12%. The detection limits in the bovine plasma were estimated as 18 ng for AMO and AMP, 25 for PENG, PENV and OXA, 3 ng for CLO and 12 ng for DICLO. Spiked plasma samples were stable for 1 wk, except for AMP and CLO, which were stable for 3 wk and OXA for 4 wk. AMO, PENG and PENV were stable for two freeze,thaw cycles, OXA, CLO and DICLO for four, while AMP only for one. [source]


Effect of selected commercial substances with cryoprotective activity on the quality of mechanically recovered, washed and frozen stored poultry meat

MOLECULAR NUTRITION & FOOD RESEARCH (FORMERLY NAHRUNG/FOOD), Issue 1 2003
J. Stangierski
Abstract Investigations were conducted on mechanically recovered poultry meat (MRPM) and on protein preparation obtained from MRPM by washing it first with 1% water solution of sodium chloride and with water afterwards. The raw materials were frozen at the temperature of ,23°C. The effect of added stabilizers on the quality of gels produced from fresh raw materials, and after freezing and frozen storage was assessed. The following additives were used: 1% pork hydrolizate (Pork Stock( 0.5% Cremodan containing carrageens, and 1.5% bovine blood plasma (AMP 600N). Freezing and frozen storage caused a significant reduction of functional properties of MRPM and its protein preparation. None of the examined additives protected simultaneously all the investigated functional properties of the frozen samples. The amount of thermal drip, the gel texture and the amount of protein transition heat were determined by scanning differential calorimetry. The lowest thermal drip in gels obtained from frozen-stored samples was observed when bovine blood plasma was used as a stabilizer. On the other hand, the most advantageous protective effect on the proteins of the frozen MRPM and on the preparation, determined by mechanical strain resistance of the gels, was found with 1% pork hydrolizate added. The results of thermodynamic investigations of proteins revealed that the best protective effect on the frozen preparation was observed with 1.5% blood plasma added. No protective activity of added Cremodan on proteins of the frozen protein preparation was noted. [source]