Stabilization of α-amylase by chemical modification with carboxymethylcellulose

✍ Scribed by Reynaldo Villalonga; Leissy Gómez; Hector L Ramírez; Maria L Villalonga

• Publisher: Wiley (John Wiley & Sons)
• Year: 1999
• Tongue: English
• Weight: 71 KB
• Volume: 74
• Category: Article
• ISSN: 0268-2575
• DOI: 10.1002/(sici)1097-4660(199907)74:7<635::aid-jctb85>3.0.co;2-m

✦ Synopsis

Carboxymethylcellulose activated by periodate oxidation was covalently linked to porcine pancreatic a-amylase (EC 3.2.1.1). The speci®c activity of the conjugate prepared was 54% of the native enzyme. The carbohydrate content was estimated to be 62% by weight as a result of the modi®cation of 67% of the amino groups from the protein. In comparison with the native enzyme, the thermostability and pH stability were improved for a-amylase by this modi®cation. The conjugate was also more resistant to the action of denaturant agents such as urea and sodium dodecylsulfate. We conclude that modi®cation of enzymes by the anionic polysaccharide carboxymethylcellulose might be a useful method for improving enzyme stability under various denaturing conditions.