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Abstract

ABSTRACT


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 LPO146s 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 10C. 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.

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