36416-81-6Relevant articles and documents
MOLECULAR GELATORS FOR CONTAINING OIL SPILLAGE
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, (2016/12/22)
The application relates to peptide-based compounds of Formula I such as the compound of Formula II, methods of making such compounds, gels comprising such compounds, methods of making gels, methods of using such compounds for containing the spill of a hydrocarbon, and methods for reclaiming solvent from gels comprising such compounds.
Low molecular weight gels: Potential in remediation of crude oil spillage and recovery
Kesava Raju, Ch. Siva,Pramanik, Bhaskar,Kar, Tanmoy,Rao, Peddy V. C.,Choudary, Nettem V.,Ravishankar, Raman
, p. 53415 - 53420 (2016/06/14)
A novel amino acid based gelator compound was developed for the phase-selective gelation of hydrocarbon solvents in a biphasic mixture with water/sea water including crude oils. With the crude oils of varying API gravity ranging from 18.7 to 40.5, the organogelator exhibited an uptake capacity ranging from 50 to 100 times. Thus, a wide range of applicabilities of the gelator to contain and mitigate oil spills of any type of crude oil covering the entire crude basket around the globe is proven for the first time.
Purification, characterization, molecular cloning, and expression of a new aminoacylase from streptomyces mobaraensis that can hydrolyze N-(Middle/Long)-chain-fatty-acyl-L-amino acids as well as N-Short-chain-acyl-L- amino acids
Koreishi, Mayuko,Nakatani, Yasuyuki,Ooi, Manami,Imanaka, Hiroyuki,Imamura, Koreyoshi,Nakanishi, Kazuhiro
experimental part, p. 1940 - 1947 (2010/07/02)
We report here on the purification, characterization, molecular cloning, and expression of a new aminoacylase, initially isolated from the supernatant of Streptomyces mobaraensis (Sm-AA). Purified wild-type Sm-AA was found to be a monomeric protein with a molecular mass of 55 kDa. The cloned gene of Sm-AA contained an ORF of 1,383 bp, encoding a polypeptide of 460 amino acids. A BLAST search revealed that Sm-AA belongs to the peptidase M20 family, with identities to a hypothetical protein from Streptomyces pristinaespiralis, a putative peptidase from Streptomyces avermitilis, peptidase M20 from Frankia sp., succinyl-diaminopimelate desuccinylase from Hemophilus influenzae, and aminoacylase-1 from porcine kidney at 89, 88, 67, 29, and 25% respectively. The Sm-AA gene was subcloned into an expression vector, pSH19, and was expressed in Streptomyces lividans TK24. The amount of the recombi- nant Sm-AA expressed in the S. lividans cells was approximately 42-fold higher than that of Sm-AA found in the supernatant of S. mobaraensis. Sm-AA showed high hydrolytic activity towards various N-acetyl-L-amino acids and N-(middle/long)-chain-fatty-acyl-L- amino acids, with a preference for the acyl derivatives of L-Met, L-Ala, L-Cys, etc. with an optimum pH and temperature for reaction of about 7.5 and 50 °C (at pH 7.5).
HIGHER N-ACYL-L-AMINO ACID DERIVATIVES
Kochetkov, K. A.,Urmambetova, Zh. S.,Belikov, V. M.,Bakasova, Z. B.
, p. 2311 - 2316 (2007/10/02)
A preparative method is proposed for obtaining higher N-acylamino acids by reaction of free amino acids with fatty acid nitrophenyl esters.It was shown that these acids can transport positive ions through a liquid lipophilic medium.A direct method is proposed for obtaining fatty acid 4-nitrophenyl esters by boiling 4-nitrophenol and the fatty acid in xylene in a Soxhlet apparatus in the presence of an acid catalyst.
