Enzyme‐catalyzed hydrolysis of 18‐methyl eicosanoic acid‐cysteine thioester

Ganske, Franka; Meyer, H.; Deutz, Herbert; Bornscheuer, Uwe T.

doi:10.1002/ejlt.200300800

Cited by 12 publications

(9 citation statements)

References 5 publications

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“…These results indicate that most lipases catalyze acylations (or transesterifications, deacylations) regioselectively only at primary hydroxy functions 34–36.…”

Section: Discussionmentioning

confidence: 87%

Enzymatic production of modified 2‐dodecyl‐sophorosides (biosurfactants) and their characterization

Recke

Gerlitzki

Hausmann

et al. 2013

Euro J Lipid Sci & Tech

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Alkyl sophorosides, a special type of sophorolipids, can be produced using Candida bombicola cultures with glucose as main carbon source and 2-dodecanol as co-substrate. The dominating component, 2-dodecylsophoroside SL-E 2-12 , was purified via medium pressure liquid chromatography (MPLC) and used as substrate for further enzymatic modifications. Using b-glucuronidase in aqueous media the first modification gave a glycosidic cleavage of the acetyl glucose unit leading to 2-dodecyl-glucoside GL-A 2-12 . In a subsequent lipase-catalyzed acylation with sebacic acid in toluene this compound was functionalized regioselectively at the primary C-6 0 position of glucose. Similar lipase-catalyzed reactions in toluene, but now using SL-E 2-12 as acyl acceptor and unusual hydroxyl fatty acids -3-hydroxy decanoic acid and 17-hydroxy stearic acid -as acyl donors, resulted in mono-and diacylations of primary hydroxyl positions of the sophorose unit (C-6 0 and C-6 00 ) as shown by NMR and MS studies. In physicochemical characterization experiments the new glycoconjugates lowered the surface tension of water from 72 to 27-32 mN/m. Moreover it was observed that the new products inhibit the growth of particular Gram-positive bacteria. Additionally they indicate potential for anti-tumor promoting activity.Practical applications: According to literature data 2-alkyl-sophorosides can be produced using Candida bombicola cultures with yields of more than 20 g/L. Based on this starting material, 2-dodecyl-sophoroside, several regioselective enzymatic modifications were performed. Initially, b-glucuronidase catalysis in aqueous buffer solution gave 2-dodecyl-glucoside which was then successfully acylated at the C-6 position of glucose by lipase catalysis using a common dicarboxylic acid, sebacic acid. The resulting free carboxylic function of the acidic derivative opens up the possibility of achieving additional chemo-enzymatic reactions at this position for conversion, for instance, into polyesters. In addition lipase catalysis in organic solvents of 2-dodecyl-sophoroside allows acylation with unusual hydroxyl fatty acids of microbial origin. Physicochemical studies showed that these new glycoconjugates may be of interest for the cosmetic industry due to moisture conservation of the skin. For practical applications the conditions of the above biocatalytic reactions have been improved and scaled up.

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“…These results indicate that most lipases catalyze acylations (or transesterifications, deacylations) regioselectively only at primary hydroxy functions 34–36.…”

Section: Discussionmentioning

confidence: 87%

Enzymatic production of modified 2‐dodecyl‐sophorosides (biosurfactants) and their characterization

Recke

Gerlitzki

Hausmann

et al. 2013

Euro J Lipid Sci & Tech

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“…Alkaline treatments (hair colorings, bleaching, perms) or sunlight can lead to a loss of 18-MEA and causes the defatting of hair. Consequently hair becomes dry and brittle and loses its springiness and luster [24]. The synthesis of 18-MEA requires the oxidative decarboxylation of isoleucine.…”

Section: -Methyl-eicosanoic Acid In Hairmentioning

confidence: 99%

Integral hair lipid in human hair follicle

Lee

2011

Journal of Dermatological Science

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“…RecGEOker Wool (100) 5 Gelatin (92) Casein (95) Albumin (37) Collagen type 1 (98) Note: Source organism, accession numbers and references can be found in Table 3; Activity normalized to the following substrates-1 keratin azure, 2 keratin; 3 Some enzymes also showed esterase activity, which may be of importance for facilitating enzyme access to the substrate. Fatty acids of the cuticle surface are linked via a thioester to the protein matrix below in keratin fibres and feathers [14]. Only three enzymes in Table 6 have been characterized on ester substrates.…”

Section: M4 Peptidasesmentioning

confidence: 99%

“…This cuticle filament-associated surface membrane is 2-7 nm thick and composed of highly cross-linked proteins and lipids. The major fatty acid of the cuticle surface lipids found in human and animal hair is 18-methyleicosanoic acid [14]. It is covalently linked to the protein matrix below by a thioester linkage and the protein matrix is cross-linked by isopeptide bonds [15].…”

mentioning

confidence: 99%

Challenges and Opportunities in Identifying and Characterising Keratinases for Value-Added Peptide Production

et al. 2020

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Keratins are important structural proteins produced by mammals, birds and reptiles. Keratins usually act as a protective barrier or a mechanical support. Millions of tonnes of keratin wastes and low value co-products are generated every year in the poultry, meat processing, leather and wool industries. Keratinases are proteases able to breakdown keratin providing a unique opportunity of hydrolysing keratin materials like mammalian hair, wool and feathers under mild conditions. These mild conditions ameliorate the problem of unwanted amino acid modification that usually occurs with thermochemical alternatives. Keratinase hydrolysis addresses the waste problem by producing valuable peptide mixes. Identifying keratinases is an inherent problem associated with the search for new enzymes due to the challenge of predicting protease substrate specificity. Here, we present a comprehensive review of twenty sequenced peptidases with keratinolytic activity from the serine protease and metalloprotease families. The review compares their biochemical activities and highlights the difficulties associated with the interpretation of these data. Potential applications of keratinases and keratin hydrolysates generated with these enzymes are also discussed. The review concludes with a critical discussion of the need for standardized assays and increased number of sequenced keratinases, which would allow a meaningful comparison of the biochemical traits, phylogeny and keratinase sequences. This deeper understanding would facilitate the search of the vast peptidase family sequence space for novel keratinases with industrial potential.Catalysts 2020, 10, 184 2 of 23 with keratinolytic activity for keratin hydrolysis protects the integrity of the keratin amino acids in most cases and allows control over the peptide size in the hydrolysate that is not readily achievable with other methods [5]. This degree of control allows the production of bespoke medical biomaterials, smart biocomposites, protein feed supplements with enhanced nutritional and bioactive properties as well as personal care products with enhanced functional and bioactive properties.Identifying peptidases with keratinolytic activity is an inherent problem associated with the search for new enzymes. Keratinase activity however appears to be dependent on the accessibility of the keratin substrate to the enzyme [6,7]. Thermochemical or biochemical treatment of the keratin, with emphasis on the reduction of the disulphide bond and disruption of other important bonds involved in the structural stability of keratin like isopeptide, hydrogen and glycolytic bonds [6,[8][9][10], appears to be the prerequisite for enzymatic hydrolysis. Sulphitolysis, which involves reduction of the disulphide bond in keratin, often acts synergistically with keratinases in nature [6,7]. Although destabilization of the keratin structure is a prerequisite for keratin hydrolysis, not all peptidases can hydrolyse keratin. Peptidases like trypsin, papain and pepsin cannot hydrolyse keratin as efficiently ...

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Enzyme‐catalyzed hydrolysis of 18‐methyl eicosanoic acid‐cysteine thioester

Cited by 12 publications

References 5 publications

Enzymatic production of modified 2‐dodecyl‐sophorosides (biosurfactants) and their characterization

Enzymatic production of modified 2‐dodecyl‐sophorosides (biosurfactants) and their characterization

Integral hair lipid in human hair follicle

Challenges and Opportunities in Identifying and Characterising Keratinases for Value-Added Peptide Production

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