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Wyświetlanie 1-3 z 3
Tytuł:
Zastosowania enzymów z tkanek zwierzęcych w syntezie organicznej i biokatalizie. Część I. Hydrolazy
Applications of hydrolases from animal tissues in organic synthesis
Autorzy:
Hibner, H.
Ostaszewski, R.
Powiązania:
https://bibliotekanauki.pl/articles/172016.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
enzymy zwierzęce
biokataliza
synteza organiczna
zastosowania hydrolaz
animal enzymes
biocatalysis
organic synthesis
applications of hydrolases
Opis:
This work presents systematically enzymes which can be obtained form animal tissue and their applications in synthesis of pharmaceuticals and nonracemic organic compounds. It lays out similarities in procedures of isolation and purification of particular enzymes. Such procedures usually are so simple that they can be used in every industrial or research laboratory. Most animal enzymes are well-investigated and their structures and substrate specificity are known. They are used as biocatalysts in many chemical processes. Others were used in one or a few reactions but their natural substrates and biochemical properties are described. Trials of predicting potential applications of such enzymes and other substrates for them were done. In this part typical applications of hydrolases: lipases (porcine pancreatic lipase [8–17], lamb pregastric lipase [22]), esterases (porcine, horse liver esterase, liver acetone powders [34–43, 46]), L-aminoacylase [48, 49], pepsin [56], trypsin [58, 59], imidase [52, 53], aldohexose hydrolases [60, 62-64], nucleotide pyrophosphatase [65]; were described. Also examples of immobilized [10, 32] or recombined [49] enzymes are given in the text. These modifications enhance catalytic properties or reduce costs of using enzymes. In practical applications a biocatalytic effect of enzymes from animal sources is often compared with microbial ones. This text is focused on processes where animal enzymes gave much better results (yield and enantioselectivity) than microorganisms. They are also proper, unlike whole microorganisms, to investigate and computer analysis of mechanism of the reaction. Enzymes isolated from animal tissues usually have well-defined structure of active site which is a key to predict mechanisms.
Źródło:
Wiadomości Chemiczne; 2011, 65, 7-8; 557-583
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Zastosowania wybranych enzymów z tkanek zwierzęcych w syntezie organicznej i biokatalizie. Część II. Oksydoreduktazy, transferazy, liazy, izomerazy
Applications of enzymes from animal tissues in organic synthesis, Part 2
Autorzy:
Hibner, H.
Ostaszewski, R.
Powiązania:
https://bibliotekanauki.pl/articles/172018.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
enzymy zwierzęce
biokataliza
synteza organiczna
zastosowania enzymów
animal enzymes
biocatalysis
organic synthesis
application of enzymes
Opis:
This work shows systematically known types of animal enzymes and their applications in synthesis of pharmaceuticals and nonracemic organic compounds. It lays out similarities in procedures of isolation and purification of particular enzymes. Such procedures usually are so simple that they can be used in every industrial or research laboratory. Most animal enzymes are well-investigated and their structures and substrate specificity are known. They are used as biocatalysts in many chemical processes. Others were used in one or a few reactions but their natural substrates and biochemical properties are described. Trials of predicting potential applications of such enzymes and other substrates for them were performed. Typical applications of: – Oxidoreductases: horse liver alcohol dehydrogenase [3–13], lactate dehydrogenase [16–18], glutamate dehydrogenase [19, 20], carbonyl reductase [24], catalase [27]; – Transferases: transaldolase [29], galactosyltransferase [30], UDP-glucuronosyltransferase [31], fucosyltransferase [34], farnesyl diphosphate synthase [35]; – Lyases: DOPA decarboxylase [38, 39], aldolase [42]; – Isomerases: N-acyl-D-glucosamine 2-epimerase [44] were described. Also examples of or recombined [24, 39, 44] enzymes are given in the text. These modifications enhance catalytic properties or reduce costs of using enzymes. In practical applications a biocatalytic effect of enzymes from animal sources is often compared with microbial ones. This text is focused on processes where animal enzymes gave much better results (yield and enantioselectivity) than microorganisms. They are also proper, unlike whole microorganisms, to investigate and computer analysis of mechanism of the reaction. Enzymes isolated from animal tissues usually have well-defined structure of active site which is a key to predict mechanisms. A quantitative analysis of applications of these enzymes was performed. Among animal enzymes hydrolases and oxidoreductases have found the most applications in synthesis. Transferases are also often used. Other classes of enzymes seldom act as biocatalysts. It is general tendency, true also in relation to microbial and plant enzymes.
Źródło:
Wiadomości Chemiczne; 2011, 65, 7-8; 585-607
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Biokatalityczne metody otrzymywania nieracemicznych alkoholi aryloallilowych
Biocatalytic methods for preparation of nonracemic arylallylic alcohols
Autorzy:
Szymkuć, S.
Ostaszewski, R.
Powiązania:
https://bibliotekanauki.pl/articles/172469.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Chemiczne
Tematy:
biokataliza
nieracemiczne alkohole aryloallilowe
synteza organiczna
enzymy
mikroorganizmy
biocatalysis
nonracemic arylallylic alcohols
organic synthesis
enzymes
microorganisms
Opis:
Different methods for preparing nonracemic arylallylic alcohols are presented in this work. A key feature was an application the biocatalyst as a mean to obtain final products. These compounds play an important role in pharmaceutical industry, because they are substrates in the synthesis of various important therapeutics [1–3]. Methods presented in this work are divided into five main groups: 1. enantioselective hydroxylation, 2. microbiological deracemization, 3. enzymatic kinetic resolution, 4. enzymatic dynamic kinetic resolution, 5. enantioselective reduction. First two methods use only microorganisms like bacteria [4, 5, 10], fungi [6–8] or yeasts [11] as biocatalysts. Owing to the metabolic processes in the cells it was possible to obtain nonracemic arylallylic alcohol (results for method 2 are presented in Table 1). Unfortunately, the data were insufficient to create direct correlation between values of enantiomeric excess and types of applied microorganisms. Methods 3 and 4 used only isolated enzymes as biocatalysts. They belong to two classes: hydrolases and oxidoreductases. Oxidoreductases were used in the enzymatic kinetic resolution based on the enantioselective oxidation [28] of one enantiomer of the racemic arylallylic alcohol. Nevertheless, hydrolases [12–27], mainly lipases, isolated from microorganisms are enzymes of common use in enzymatic kinetic resolution. Owing to this method it was possible to obtain final products with excellent enantioselectivity (results are presented in Tables 2 and 3). Because kinetic resolution and dynamic kinetic resolution are related processes, in most cases similar enzymes are used. The choice of lipases as biocatalysts for method 4 was caused by the fact that they are able to catalyze enantioselective transesterification of arylallylic alcohols or their acetates. Furthermore, racemization is very important factor for efficacy of dynamic kinetic resolution processes. In most cases they are catalyzed by different types of complexes based on palladium [30, 31] and ruthenium [32, 34]. Final products prepared by this method had very high enantiomeric excesses and yields up to 93% (results are presented in Tables 4 and 5). The only method, presented in this work, that allowed to use both enzymes [39–41] and microorganisms [35–38] as biocatalysts, was enantioselective reduction. This method allows to obtain nonracemic arylallylic alcohols with excellent enantiomeric excess and yields up to 85% (results are presented in Table 6). In summary, all methods presented in this work show the advantages of biocatalysis as an alternative route to traditional chemical method
Źródło:
Wiadomości Chemiczne; 2012, 66, 1-2; 93-118
0043-5104
2300-0295
Pojawia się w:
Wiadomości Chemiczne
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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