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

Enhanced Stability of a Microbial Lipase Immobilized to a Novel Synthetic Amine Polymer

Bacillus sp. No. 106, which was isolated from soil, secreted an enzyme that hydrolyzed cyclo(Gly-Gly). The enzyme was purified to the ultracentrifugally homogeneous state and an activity more than 450-fold that of culture broth. The enzyme was activated by Na+, Mg2+, Ca2+, and Sr2+, and strongly inhibited by Ni2+, Cu2+, p-chloromercuribenzoate, and monoiodoacetic acid. The Km value for cyclo(Gly-Gly) was estimated to be 11.1 mM. The enzyme hydrolyzed only cyclo(Gly-Gly) among various diketopiperazines tested. Aslo, the enzyme was inert toward Gly-Gly, milk casein, and hemoglobin.

Purification and Some Properties of Cyclo(Gly-Gly) Hydrolase from a Strain of Bacillus sp. No. 106

Carboxylesterase from Ochrobactrum anthropi was purified to homogeneity by a combination of DEAE-cellulose, Sephadex G-100, and hydroxy apatite column chromatographies. The molecular weight of the enzyme was calculated to be 58,000 by Sephadex G-75 gel filtration. SDS-polyacrylamide gel electrophoresis showed that the enzyme consisted of two identical subunits with a molecular weight of 30,000. The enzyme was inactivated by several organophosphates and sulfhydryl reagents. The esterase hydrolyzed only acetate and propionate esters. In the presence of Triton X-100, the esterase hydrolyzed l-menthyl acetate but not its optical isomer. This result suggests that the enzyme can be used for the optical resolution of l-menthol.

Purification and Properties of Carboxylesterase from Ochrobactrum anthropi.

Since it was demonstrated that bitter peptides were produced from casein by the hydrolytic action of various proteases,1} some workers have reported that hydrolysis of proteins with proteolytic enzymes is usually accompanied by the formation of bitter peptides which make foods unpalatable.2 ~ 5) Studies6'7* on the structure-taste relationship of bitter peptides demonstrated that some peptides consisting of hydrophobic amino acids have the bitterness generally and that the substrate specificity of proteases which have strong affinities to hydrophobic amino acids causes the formation of such bitter peptides. Therefore, to suppress the formation of the bitter peptides in the proteolytic digests of proteins, it is useful to obtain the proteases having strong affinities for hydrophilic amino acids. In our preceding paper,8} we reported that Micromonospora melanosporea IFO 12515 secreted two poly(glutamic acid) hydrolases (PGH-I and II) of which PGH-II was purified to an electrophoretically homogeneous state at a yield of 2.3% by ion exchange chromatography followed by isoelectric focusing and gel filtration. This study deals with the enzymatic properties and mode of action of PGH-II, using either poly-Glu or poly-Glu hydrolysate as a substrate. In the enzyme assay, the reaction was done at 40 °C and pH 9.0 with 0.5% poly-Glu (Peptide Institute, Inc., Osaka). After incubation for an appropriate time, the

Yoshio Tominaga

Papers

Enhanced Stability of a Microbial Lipase Immobilized to a Novel Synthetic Amine Polymer

Purification and Some Properties of Cyclo(Gly-Gly) Hydrolase from a Strain of Bacillus sp. No. 106

Purification and Properties of Carboxylesterase from Ochrobactrum anthropi.

Some Properties and Action of Poly(glutamic acid) Hydrolase II from Micromonospora melanosporea IFO 12515

Lipase-catalyzed esterification of mono- and oligoglycosides with various fatty acids