Wyniki wyszukiwania - Biblioteka Nauki

Nowa wersja platformy, zawierająca wyłącznie zasoby pełnotekstowe, jest już dostępna.
Przejdź na https://bibliotekanauki.pl

Ograniczanie wyników

1 Journal of Ecological Engineering

1 2020

Znaleziono wyników: 1

Liczba wyników na stronie

Wyniki wyszukiwania

Sortuj według:

Ogranicz wyniki do:

A Promising Way to Dispose of Fatty Waste by Hydrolysis and Study of the Conditions for Immobilization of Rhizopus Japonicus Lipase on Carriers

100%

Skliar V. , Krusir G. , Shunko H. , Zakharchuk V. , Malovanyy M.

tom Vol. 21, nr 2

201--208

The hydrogenation process in oil and fat production is accompanied by the formation of a large amount of waste, the majority of which includes spent catalysts and spent sorbents. The 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 the 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 for the 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 one, which is a high indicator of the preservation of activity.