A review on biodiesel production using catalyzed transesterification

Biodiesel fuel production by transesterification of oils.

Biodiesel processing and production

Industrial applications of microbial lipases

https://seniordesign.engr.uidaho.edu/2007_2008/frenchfryfuel/Biodiesel%20from%20WVO%20Part%201.pdf

Biodiesel production from waste cooking oil: 1. Process design and technological assessment

A process for efficiently producing a fatty acid ester at a low cost in a system which is completely or almost completely free form any solvent In the above process, a linear lower alcohol is reacted with lipase and a fat/oil while controlling the concentration of the linear lower alcohol to a level not exceeding the lipase inhibitory concentration of the linear lower alcohol, or a fatty acid ester is added to the reaction system and lipase and a fat/oil are reacted with a linear lower alcohol By using a natural fat/oil (a vegetable fat/oil, an animal fat/oil, etc) or a waste fat/oil thereof as the above-described fat/oil, the waste fat/oil to be discharged into the environment can be recycled and, at the same time, a bio-diesel fuel with little environmental pollution can be provided

Process for producing lower alcohol ester

PROBLEM TO BE SOLVED: To provide a method for producing a xanthophyll educt from a xanthophyll ester or a composition containing the same, simply and in a good efficiency. SOLUTION: This method for producing the xanthophyll educt is constituted by allowing a lipase to act on a suspension consisting of the xanthophyll ester or the composition containing the same, water and an alcohol for converting the xanthophylls ester to the xanthophyll educt.

New method for producing xanthophyll educt and method for purifying the same

A unique enzyme from Saccharothrix sp. catalyzing D-amino acid transfer.

In this chapter, the authors describe the gene cloning, structures, and production mechanisms of microbial lipases and their production by recombinant microbes. The total RNA was extracted with 4 M guanidine thiocyanate solution from log-phase cells showing the maximum rate of specific lipase production. The primary structures of bacterial lipases were deduced from the nucleotide sequences of the cloned genes. Moreau et al. carried out the following chemical modification to investigate the role of serine in the common sequence: Ser-152 of porcine pancreatic lipase in the common sequence was specifically modified with diethyl p-nitrophenyl phosphate. Iizumi et al. attempted the lipase overproduction by a self-cloning system of KWI-56. Rhizomucor miehei lipase is synthesized as a precursor, with a signal sequence, a propeptide, and a mature enzyme. The analysis of the NH2-terminal amino acid sequence indicated that the precursor containing the propeptide was processed in and secreted from a recombinant A.

Microbial lipase: structure and production.

A unique enzyme with some properties favorable for the synthesis of D-amino acid-containing peptides has been purified from the culture broth of Saccharothrix sp. AS-2. The purification steps included ammonium sulfate fractionation, chromatographies on CM-Toyopearl 650M and ProtEx Butyl, and sucrose density-gradient isoelectric focusing. The enzyme, consisting of four subunits of 56 kDa, showed its maximum transfer activity at around pH 8.2 and 35 degrees C, and had an isoelectric point of 5.8. The enzyme yielded homooligomers from methyl esters of D-Asp(OMe), D-Met, D-Phe, D-Trp, D-Tyr, and L-Glu(OMe), but showed no hydrolytic activity toward any of the D- or L-amino acid methyl esters tested. The homooligomers were not formed from the corresponding free amino acids. The reaction of Ac-D-Phe-OMe with DL-Ala-NH(2), DL-Leu-NH(2), DL-Phe-NH(2), or DL-Trp-NH(2) was effectively catalyzed by the enzyme, both the DD- and DL-stereoisomers of the expected N-acetyldipeptide being yielded. The resulting dipeptides remained unhydrolyzed even after 48 h incubation. Also, it showed no detectable hydrolytic activity toward casein, diastereomers of diAla, diMet, and diPhe, D-/L-amino acid amides, or D-/L-amino acid p-nitroanilides, indicating that the enzyme had no peptidase activity leading to secondary hydrolysis of the growing peptide. The enzyme activity was strongly depressed by phenylmethanesulfonyl fluoride, but not by penicillin G or ampicillin, suggesting that the protein is a serine enzyme lacking penicillin-binding ability. These observations lead us to the conclusion that the enzyme from Saccharothrix sp. AS-2 characterized in this study is a new type of aminoacyltransferase with an amino acid ester as the acyl donor, and has potential utility as a catalyst for the synthesis of D-amino acid-containing peptides.

Akio Sugihara

Papers

Process for producing lower alcohol ester

New method for producing xanthophyll educt and method for purifying the same

A unique enzyme from Saccharothrix sp. catalyzing D-amino acid transfer.

Microbial lipase: structure and production.

A new type of aminoacyltransferase from Saccharothrix sp. AS-2 favorable for the synthesis of D-amino acid-containing peptides.