Study On Abalone Visceral Collagen Peptide Preparation And Extracorporeal Antioxidant Activity

In recent years，with the continuous development of abalone industry，theprocessing of abalone’s viscera is very imperative. There is a lot of collagen withvarious functions in abalone visceral connective tissue. Several parts were discussedin this paper，including process optimization of non-collagenous protein removal、process of collagen extraction、process optimization of collagen peptide manufacturewith enzyme hydrolysis、process optimization of collagen peptide decoloring、establishment of the enzyme solution dynamic model and verification of oxidationresistance of abalone visceral connective tissue collagen.1、Through single factor experiments，NaOH was identified as the reagent thatcould remove non-collagenous protein well. The effects of different immersion time、different proportions、and different NaOH concentrations on non-collagenous proteinremoval were studied by single factor experiments and orthogonal experiment. Theresults showed that: immersion time and NaOH concentration had significant impactwhile proportion did not have significant impact；the optimum conditions to removenon-collagenous protein were determined as: immersion time6h、proportion1:8、andNaOH concentration0.10mol/l.2、Through single factor experiments，collagen extraction by acid and enzymewas studied respectively. The results showed that: the best process of collagenextraction by acid was determined as: acetic acid concentration0.5mol/l、proportion1:10、and time48h and the best process of collagen extraction by enzyme wasdetermined as: pH2.5、enzyme quantity0.5%、proportion1:8、and time48h3、The effects of different time、different pH、different temperature and differentproportions of enzyme to substrate on hydrolysis degree were studied by adoptingsingle factor experiments and orthogonal experiment. The results showed that: pH andtemperature had very significant impacts and proportion of enzyme to substrate hadsignificant impacts. The optimum hydrolysis conditions were determined as:time5h、pH8.0、temperature50℃、and proportion of enzyme to substrate1.5%.4、Through a series of experiments，mechanism of hydrolyzing collagen by trypsin was explored，and the enzyme hydrolysis dynamic model was deduced according to thismechanism. The trypsin hydrolysis dynamic model was identified after the parameterswere worked out through experiment data fitting. The results showed that: mechanismof hydrolyzing collagen by trypsin was substrate inhibition and second-order kinetics for enzymedeactivation. The trypsin hydrolysis dynamic model was as follow:5、The effects of different pH、different activated carbon quantity、different timeand different temperature on collagen peptide decoloring，the reductive activity，thescavenging activity on superoxide free radical，inhibitory ability of liuid oxidation、and Fe²⁺-chelating ability of collagen peptide were studied. The results showed that:the optimum decoloring conditions were determined as: pH3.5、activated carbonquantity0.7%、temperature50℃and time60min；collagen peptide from abalonevisceral connective tissue had oxidation resistance.