教師資料查詢 | 類別: 期刊論文 | 教師: 梁慈雯 TZU-WEN LIANG (瀏覽個人網頁)

標題:Optimization of conditions for protease production by Chryseobacterium taeanense TKU001
學年96
學期2
出版(發表)日期2008/06/01
作品名稱Optimization of conditions for protease production by Chryseobacterium taeanense TKU001
作品名稱(其他語言)
著者Wang, San-lang; Yang, Chun-hsiang; Liang, Tzu-wen; Yen, Yue-horng
單位淡江大學化學學系
出版者Amsterdam: Elsevier BV
著錄名稱、卷期、頁數Bioresource Technology 99(9), pp.3700-3707
摘要A protease-producing bacterium was isolated and identified as Chryseobacterium taeanense TKU001. An extracellular metalloprotease with novel properties of solvent- and surfactant-stable was purified from the culture supernatant of C. taeanense TKU001 with shrimp shell wastes as the sole carbon/nitrogen source. The optimized condition for protease production was found when the culture was shaken at 37 °C for 3 days in 50 mL of medium containing 0.5% shrimp shell powder (SSP) (w/v), 0.1% K2HPO4, and 0.05% MgSO4 · 7H2O. 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.;The optimum pH, optimum temperature, pH stability, and thermal stability of TKU001 protease FI were 8, 60 °C, pH 6–9, and 60 °C, respectively. The optimum pH, optimum temperature, pH stability, and thermal stability of TKU001 protease FII were 7, 60 °C, pH 7–9, and 50 °C, 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 °C in the presence of 25% most tested organic solvents. Additionally, the TKU001 protease FI retained 79%, 80%, and 110% of its original activity in the presence of 2% Tween 20, 2% Tween 40, and 2% Triton X-100, respectively. However, at the same condition, the activity of TKU001 protease FII retained 100%, 100%, and 121% of its original activity, respectively. This is the first report of C. taeanense being able to use shrimp shell wastes as the sole carbon/nitrogen source for proteases production. 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.
關鍵字Chryseobacterium taeanense; Protease; Shrimp shell wastes
語言英文
ISSN0960-8524
期刊性質國外
收錄於SCI;EI
產學合作
通訊作者Wang, San-lang
審稿制度
國別荷蘭
公開徵稿
出版型式紙本
相關連結
Google+ 推薦功能,讓全世界都能看到您的推薦!