Ong Chong-Boon, Annuar Mohamad S M
a Faculty of Science , Institute of Biological Sciences, University of Malaya , Kuala Lumpur , Malaysia.
Prep Biochem Biotechnol. 2018 Feb 7;48(2):181-187. doi: 10.1080/10826068.2018.1425707. Epub 2018 Feb 20.
Immobilization of cross-linked tannase on pristine multiwalled carbon nanotubes (MWCNT) was successfully performed. Cross-linking of tannase molecules was made through glutaraldehyde. The immobilized tannase exhibited significantly improved pH, thermal, and recycling stability. The optimal pH for both free and immobilized tannase was observed at pH 5.0 with optimal operating temperature at 30°C. Moreover, immobilized enzyme retained greater biocatalytic activities upon 10 repeated uses compared to free enzyme in solution. Immobilization of tannase was accomplished by strong hydrophobic interaction most likely between hydrophobic amino acid moieties of the glutaraldehyde-cross-linked tannase to the MWCNT.
已成功将交联单宁酶固定在原始多壁碳纳米管（MWCNT）上。单宁酶分子通过戊二醛进行交联。固定化单宁酶在pH稳定性、热稳定性和循环稳定性方面均有显著提高。游离单宁酶和固定化单宁酶的最佳pH均为5.0，最佳操作温度为30℃。此外，与溶液中的游离酶相比，固定化酶在重复使用10次后仍保留了更高的生物催化活性。单宁酶的固定化很可能是通过戊二醛交联单宁酶的疏水氨基酸部分与MWCNT之间的强疏水相互作用实现的。
