Isolation And Identification Of One Intestinal Bacteria Producing Collagenase

Collagen is a kind of white opacity native celloglobulin without branched chain. With itstriple helix structure, Collagen is too stable to be decomposed and assimilated. When thecollagen is hydrolyzed into collagen peptide, the digestion and absorption would get easier.The best way of the preparation of collagen peptide is hydrolysis by collagenase. With thedevelopment of the methods of extracting collagen protein and deep research of its structureand properties, the functional properties of collagen and its peptide are widely realized, theresearch and application of collagen have become a hotspot in biological and food industry,medical industry, etc.The main contents are screening a high activity strain producing collagenase fromintestine of a sebasttodes fuscescerns and investigating the fermentation of the screened strainand the characteristies of collagenase from the strain including its reaction condition and itsthermo stability. It should provide a new way for industrial production of collagen peptide.A high activity strain was screened through screening and secondary screening after thesimple treatment of the sebasttodes fuscescerns. According to the characteristics ofmorphology, physiology and biochemistrytests, the strain was similar to belong to Aeromonas.The strain was temporarily named Aeromonas sp.F3.The fermentation of Aeromonas sp.F3was investigated through single-factor test. Themain factors included fermentation conditions and the medium. With the test, the optimalculture condition was determined:40°C of fermentation temperature, pH8and volume80~100mL/250ml for24h. The optimal liquid medium was:3g/L glucose as carbon source,9g/L yeast extract powder as nitrogen source,5g/L NaCl as inorganic salt and10mg/LMnSO4as metal ion. Under the optimum condition, the enzyme activity increased veryobservably.The characteristies of collagenase from Aeromonas sp.F3including its reaction conditionand its thermostability were investigated through single-factor test. Thermal treatment at50°C for40min resulted in obvious deactivation. With single factor trial, the optimal condition was determined. Its optimum reaction temperature was40°C and pH value was8.6.Collagenase activity was activated when0.5mmol/L Ca2+existed. The hydrolysis was veryobservably with the optimal condition.