72-08-2

Basic information

• Product Name: L-LACTIC ACID, 40% SOLN
• Synonyms: L-LACTIC ACID, 40% SOLN
• CAS NO: 72-08-2
• Molecular Formula: C₃H₅O₃
• Molecular Weight: 90.07794
• Mol File: 72-08-2.mol

Chemical Properties

• Appearance: /
• CAS DataBase Reference: L-LACTIC ACID, 40% SOLN(CAS DataBase Reference)
• NIST Chemistry Reference: L-LACTIC ACID, 40% SOLN(72-08-2)
• EPA Substance Registry System: L-LACTIC ACID, 40% SOLN(72-08-2)

Safety Data

• Hazardous Substances Data: 72-08-2(Hazardous Substances Data)

Upstream product

• 50-99-7 D-glucose 
• 108-91-8 cyclohexylamine 
• 1002754-96-2 C₂₀H₃₈N₆O₇S 
• 41656-56-8 (S)-D-lactoylglutathione 

Downstream Products

• 57-55-6 propylene glycol 

Relevant articles and documents

The crystal structure of a homodimeric Pseudomonas glyoxalase I enzyme reveals asymmetric metallation commensurate with half-of-sites activity

The Zn inactive class of glyoxalase I (Glo1) metalloenzymes are typically homodimeric with two metal-dependent active sites. While the two active sites share identical amino acid composition, this class of enzyme is optimally active with only one metal per homodimer. We have determined the X-ray crystal structure of GloA2, a Zn inactive Glo1 enzyme from Pseudomonas aeruginosa. The presented structures exhibit an unprecedented metal-binding arrangement consistent with half-of-sites activity: one active site contains a single activating Ni2+ ion, whereas the other contains two inactivating Zn2+ ions. Enzymological experiments prompted by the binuclear Zn2+ site identified a novel catalytic property of GloA2. The enzyme can function as a Zn2+/Co2+ -dependent hydrolase, in addition to its previously determined glyoxalase I activity. The presented findings demonstrate that GloA2 can accommodate two distinct metal-binding arrangements simultaneously, each of which catalyzes a different reaction.

Fermentation process using yeast cells having disrupted pathway from dihydroxyacetone phosphate to glycerol

In a fermentation process, a cell of a pre-whole genome duplication yeast, which is genetically modified to delete or disrupt a native metabolic pathway from dihydroxyacetone phosphate to glycerol, is cultivated under fermentation conditions and in the presence of a carbon source to produce a desired fermentation product, wherein the glycerol yield is less than 2% based on the weight of the carbon source that is consumed by the cell, and whereby glycerol is added to the fermentation medium.

Ni2 +-activated glyoxalase i from Escherichia coli: Substrate specificity, kinetic isotope effects and evolution within the βαβββ superfamily

The Escherichia coli glyoxalase system consists of the metalloenzymes glyoxalase I and glyoxalase II. Little is known regarding Ni 2 +-activated E. coli glyoxalase I substrate specificity, its thiol cofactor preference, the presence or absence of any substrate kinetic isotope effects on the enzyme mechanism, or whether glyoxalase I might catalyze additional reactions similar to those exhibited by related βαβ ββ structural superfamily members. The current investigation has shown that this two-enzyme system is capable of utilizing the thiol cofactors glutathionylspermidine and trypanothione, in addition to the known tripeptide glutathione, to convert substrate methylglyoxal to non-toxic d-lactate in the presence of Ni2 + ion. E. coli glyoxalase I, reconstituted with either Ni2 + or Cd2 +, was observed to efficiently process deuterated and non-deuterated phenylglyoxal utilizing glutathione as cofactor. Interestingly, a substrate kinetic isotope effect for the Ni 2 +-substituted enzyme was not detected; however, the proton transfer step was observed to be partially rate limiting for the Cd 2 +-substituted enzyme. This is the first non-Zn 2 +-activated GlxI where a metal ion-dependent kinetic isotope effect using deuterium-labelled substrate has been observed. Attempts to detect a glutathione conjugation reaction with the antibiotic fosfomycin, similar to the reaction catalyzed by the related superfamily member FosA, were unsuccessful when utilizing the E. coli glyoxalase I E56A mutein.

Substrate and reaction intermediate mimics as inhibitors of 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase

3-Deoxy-d-arabino-heptulosonate 7-phosphate (DAH7P) synthase catalyses the aldol-like addition of phosphoenolpyruvate (PEP) to d-erythrose 4-phosphate in the first step of the shikimate pathway to aromatic amino acids. A series of compounds, designed to m

Modelling of the periodic anaerobic baffled reactor (PABR) based on the retaining factor concept

The fact that the active biomass is continuously removed from the continuously stirred anaerobic digesters, leading to long retention times, has been overcome in a number of high rate systems based on immobilization of the active biomass, such as the Upflow Anaerobic Sludge Blanket Reactor (UASBR) and the Anaerobic Baffled Reactor (ABR). A kinetic model of glucose consumption, which was developed based on a batch kinetic experiment, was used for the development of a dynamic model for the prediction of the behaviour of the recently developed flexible reactor called the Periodic Anaerobic Baffled Reactor (PABR). The PABR may be operated as a UASBR, an ABR or at an intermediate mode. The key assumption of the model is that the hydraulic behaviour of a PABR is equivalent with the behaviour of CSTRs in series as concerning the dissolved matter, whereas the biomass is allowed to be retained in the PABR through a retention factor accounting for precipitation. The model adequately predicted the experimental behaviour of a glucose fed PABR. The model was subsequently used to examine the behaviour of the PABR as a function of operating conditions, both for constant and varying loading rates. It was shown that for different cases, the reactor should best be operated as a UASBR or as an ABR. The fact that the active biomass is continuously removed from the continuously stirred anaerobic digesters, leading to long retention times, has been overcome in a number of high rate systems based on immobilisation of the active biomass, such as the Upflow Anaerobic Sludge Blanket Reactor (UASBR) and the Anaerobic Baffled Reactor (ABR). A kinetic model of glucose consumption, which was developed based on a batch kinetic experiment, was used for the development of a dynamic model for the prediction of the behaviour of the recently developed flexible reactor called the Periodic Anaerobic Baffled Reactor (PABR) [(1998) Wat. Sci. Technol. 38(8-9), 401- 408]. The PABR may be operated as a UASBR, an ABR or at an intermediate mode. The key assumption of the model is that the hydraulic behaviour of a PABR is equivalent with the behaviour of CSTRs in series as concerning the dissolved matter, whereas the biomass is allowed to be retained in the PABR through a retention factor accounting for precipitation. The model adequately predicted the experimental behaviour of a glucose fed PABR. The model was subsequently used to examine the behaviour of the PABR as a function of operating conditions, both for constant and varying loading rates. It was shown that for different cases, the reactor should best be operated as a UASBR or as an ABR. (C) 2000 Elsevier Science Ltd.