摘要：Lactoperoxidase (LPO) could be simply obtained from whey through immobilization using a cation exchange resin of SP Sepharose. LPO received high attention since the antimicrobial properties of LPO system (LPOS) that are consisted of LPO, SCN¯ and H2O2 was able to generate OSCN¯ for strong antimicrobial agents. This study was done to analyze the immobilization efficiency of LPO onto two types of sepharose: SP-Sepharose Fast Flow (SPFF) and SP-Sepharose Big Beads (SPBB). The remaining of LPO’s activity (%) against storage solution was also observed. The whey was obtained from bovine skimmed milk that was coagulated using rennet and acid lactic. The LPO was obtained from whey using SPFF. To analyze the resistence of enzyme activity, the immobilized LPO was stored in pure water, phosphate buffer, milk and whey at 10°C. The activity of LPO was monitored for 10 days. The result indicates that the LPO could be purified from whey and single band has been detected using electrophoresis method. The obtained LPO (35 U mL-1) was attached onto SPFF and SPBB. Maximum immobilization efficiency has been achieved by 0.6 g SP-FF and 0.9 g SP-BB. LPO activity of the immobilized LPO were able to be kept until 5 days when it was stored in whey. Other storage solution remained various LPO activity during storage. This study concluded that IE of LPO attached onto sepharoses might be reached variously depended on the sepharose type and whey as LPO source might be used for maintaining LPO activity.
