An extracellular metalloprotease with novel properties of solvent- and surfactant-stable was purified from the culture supernatant of Chryseobacterium taeanense TKU001 with shrimp shell wastes as the sole carbon/nitrogen source. Two extracellular proteases (FI and FII) were purified and characterized, and their molecular weights, pH and thermal stabilities were determined. The molecular masses of TKU001 protease FI and FII determined by SDS-PAGE and gel filtration were approximately 41 kDa and 75 kDa, respectively. TKU001 protease FI and FII were both inhibited completely by EDTA, indicating that the TKU001 protease FI and FII were metalloproteases. TKU001 protease FI and FII retained more than 75% of its original protease activity after preincubation for 10 days at 4.degree.C in the presence of 25% most tested organic solvents. The novelties of the TKU001 protease include its high stability to the solvents and surfactants. These unique properties make it an ideal choice for application in detergent formulations and enzymatic peptide synthesis.
2007年 台灣幾丁質幾丁聚醣研討會論文集=Proceedings of 2007 Taiwan Chitin and Chitosan Symposium, 3p.