Preparation And Properties Of Soluble Matrix Of Ostrea Plicatula Gmelin Shell

The soluble matrix (SM) of Ostrea plicatula Gmelin shell was first studied in this thesis. The SM was isolated from shell with 2% acetic acid. The percentage of SM was 0.16% by weight in dry shell. The content of protein, carbohydrate and phosphate was 67. 03%, 5. 26% and 15.05% in SM, respectively. The SM was separated into two fractions: SE I and SE II by DEAE-cellulose ion-exchange chromatography and Sephacryl S-300 gel permeation chromatography. SE I and SE II were obtained and lyophilized to dry powder.The content of protein were assayed in SE I and SEII, which was 63. 52 % and 72. 24% by weight, respectively. The contents of carbohydrate and phosphate were 18. 37%, 3. 72% and 15. 56%, 8.16% by weight in SE I and SEII, respectively. The molecular weight of SE I and SEII were assayed by gel permeation chromatography and polyacrylamide gradient gel electrophoresis. The molecular weight of SE I was 580700D and 578100D by the two methods, while the molecular weight of SEII was 50800D and 50900D, respectively. The results of molecular weight was close in the two methods. SE I and SEII were assayed to be single component by PAGE and were proved to be glycoproteins stained by PAS. Infrared spectra also indicate that the absorb characteristic of the two fractions were same as the glycoproteins. SE I and SEII were rich in Asp acids by amino acid analyses , the content of Asp was 27.65% and 31.04%, respectively. PC showed that glucose was the main sugar component in SE I and SEII. Thelinkage between the glyean and protein may be of 0-glycosidic linkage in SE I .The scale inhibition on CaC03 of SM was studied on solution conductivity measurement. The results showed that the best conditions for scale inhibition was: the concentration of SM was 8 mg. L-1, temperature 30C, pH8. 5. At the same concentration of the inhibitor , the scale inhibition of SM was better than PAM and HAMP. The scale inhibition of SM was better in water than in synthetic sea water.Optimum conditions of mineral protein salt chelated with Zinc was studied. The results showed that the best conditions for the chelation was: the concentration of protein was 0. Olg. ml-1, the mass ratio of protein to Zinc 2:1, pH7.0, temperature 40C and the chelate time 40min.