PMID: 7281254Jul 1, 1981

Immobilization of Penicillium vitale catalase on aminoethyl cellulose and properties of the obtained preparations

Ukrainskiĭ biokhimicheskiĭ zhurnal
N V LatyshkoM F Gulyĭ

Abstract

Preparations of Penicillium vitale catalase immobilized by aminoethyl cellulose (AE-cellulose) are obtained using two methods: by the enzyme covalent cross-linking with the carrier by glutaric aldehyde and by the covalent binding of catalase to the carrier aminogroups through the carbohydrate enzyme component. A dependence is established for the degree of catalase binding and catalase activity of the immobilized enzyme on the enzyme carrier in immobilization ratio. The optimal enzyme-carrier ratio in both cases is 10 mg of the enzyme per 1 g of the carrier. With such a ratio and binding by means of glutaric aldehyde 9.5 +/- 0.23 mg of protein is added to 1 g of the carrier with the 68.7 +/- 3.45% of the activity preserved, and in binding through the carbohydrate component of catalase 9.2 +/- 0.29 mg/g is added with preservation of 84.7 +/- 4.42% of the activity. Studies in properties of soluble and AE-cellulose immobilized catalase of P. vitale and determination of thermodynamic parameters of inactivation showed that the immobilized enzyme is more stable to the effect of temperature and extreme pH values than the soluble one.

Related Concepts

aminoethyl cellulose
Catalase T
Sulfite Cellulose
Penicillium

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