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Preparation and Activity of Antimicrobial Peptides from Bovine Bone Collagen |
ZHANG Shun-liang;CHENG Xiao-yu;PAN Xiao-qian;QIAO Xiao-ling;CHEN Wen-hua |
China Meat Research Center, Beijing 100068, China |
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Abstract Seven different proteases, pepsin, alkaline protease, neutral protease, trypsin, protamex, flavourzyme and papain, were compared for their effectiveness in hydrolyzing bovine bone collagen. The resulting hydrolysates were centrifugated and the supernatants were vacuum freeze dried and tested for antimicrobial activity against Staphyloccocus aureus and Salmonella enteritidis. Protamex was found to provide maximum degree of hydrolysis among the proteases, and the optimal conditions for hydrolyzing bovine bone collagen with it were determined as 1.25%of enzyme dosage (relative to the weight of bovine bones) and 4 h of hydrolysis time. The hydrolysates obtained using flavourzyme and neutral protease had an inhibitory effect on Staphyloccocus aureus with an inhibition zone diameter of 6.03 mm and 7.97 mm, respectively, whereas those obtained using protamex, flavourzyme and trypsin could inhibit Salmonella enteritidis with an inhibition zone diameter of 8.67, 9.10 mm and 9.03 mm, respectively.
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