A Promising Way to Dispose of Fatty Waste by Hydrolysis and Study of the Conditions for Immobilization of Rhizopus Japonicus Lipase on Carriers
 
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1
Odessa National Academy of Food Technologies
2
Odessa National Economic University
3
Lviv Polytechnic National University
CORRESPONDING AUTHOR
Viktoriia Skliar   

Odessa National Academy of Food Technologies
Publication date: 2020-02-01
 
J. Ecol. Eng. 2020; 21(2)
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ABSTRACT
The hydrogenation process in oil and fat production is accompanied by the formation of a large amount of waste, the main of which are spent catalyst and spent sorbent. Bioconversion of lipids through the use of immobilized enzyme preparations expands the possibilities and is one of the most powerful resource potentials of environmental biotechnology. Bioconversion of lipids through the use of immobilized enzyme preparations expands the possibilities and is one of the most powerful resource potentials of environmental biotechnology. The adsorption methods are most effective, which is due to the ease of the binding process, the low cost of the carrier and the absence of toxic substances. Immobilization of adsorption provides a large surface area, which is important for lipolytic enzymes performing catalysis at the interface. In most cases, adsorption slightly reduces the activity of lipases and, which is extremely important, does not affect their specificity. It was shown that the use of activated carbon with a grain size of 2.0-2.8 as a carrier for immobilization of lipase, leads to maximum preservation of the initial lipolytic activity. The weight ratio of carrier/ enzyme, optimal in terms of preservation of lipolytic activity, was 1 g of biopolymer carrier per 500 mg of lipase (1: 0.5) with preservation of 36.33% of the initial activity of the native enzyme. From the obtained experimental data, it follows that the rational conditions of immobilization of Rhizopus japonicus is GM 1.5, temperature 25 ° С, duration of immobilization 15 minutes, the size of particles of activated carbon as a matrix is 2.0-2.8 mm. The lipolytic activity of the enzyme immobilized under these conditions is preserved by more than 30% compared with the native, which is a high indicator of the preservation of activity.