Name: | Tetrahydrofurfuryl alcohol |
Synonyms: | Tetrahydro-2-furanmethanol; THFA; (+/-)-Tetrahydrofurfuryl alcohol; (+/-)-2-(Hydroxymethyl)tetrahydrofuran; TETRAHYDROFURFURYLIC ALCOHOL; Tetrahydrofuryl Alcohol |
CAS: | 97-99-4 |
EINECS: | 202-625-6 |
Molecular Formula: | C5H10O2 |
Molecular Weight: | 102.13 |
InChI: | InChI=1/C5H10O2/c6-4-5-2-1-3-7-5/h5-6H,1-4H2 |
Molecular Structure: | |
Properties | |
Density: | 1.0543 |
Stability: | Stable under normal temperatures and pressures. |
Refractive index: | 1.451-1.453 |
Water Solubility: | soluble |
Solubility: | soluble |
Appearance: | Colorless to light yellow liquid |
Specification: |
Tetrahydrofurfuryl alcohol (CAS No.97-99-4), it also can be called Tetrahydro-2-furanmethanol ; THFA .
Tetrahydrofurfuryl alcohol (CAS No.97-99-4) is a clear colorless liquid with a mild odor. its flash point 167°F, its vapors are heavier than air, it is denser than water and it is soluble in water . Tetrahydrofurfuryl alcohol (CAS No.97-99-4),inhalation or contact with it may irritate or burn skin and eyes. Fire may produce irritating, corrosive and/or toxic gases. Vapors may cause dizziness or suffocation. Runoff from fire control or dilution water may cause pollution. An organism tentatively identified as Ralstonia eutropha was isolated from enrichment cultures containing Tetrahydrofurfuryl alcohol (THFA) as the sole source of carbon and energy. The strain was able to tolerate up to 200 mM THFA in mineral salt medium. The degradation was initiated by an inducible ferricyanide-dependent alcohol dehydrogenase (ADH) which was detected in the soluble fraction of cell extracts. The enzyme catalyzed the oxidation of THFA to the corresponding tetrahydrofuran-2-carboxylic acid. Studies with n-pentanol as the substrate revealed that the corresponding aldehyde was released as a free intermediate. The enzyme was purified 211-fold to apparent homogeneity and could be identified as a quinohemoprotein containing one pyrroloquinoline quinone and one covalently bound heme c per monomer. It was a monomer of 73 kDa and had an isoelectric point of 9.1. A broad substrate spectrum was obtained for the enzyme, which converted different primary alcohols, starting from C2 compounds, secondary alcohols, diols, polyethylene glycol 6000, and aldehydes, including formaldehyde. A sequence identity of 65% with a quinohemoprotein ADH from Comamonas testosteroni was found by comparing 36 N-terminal amino acids. The ferricyanide-dependent ADH activity was induced during growth on different alcohols except ethanol. In addition to this activity, an NAD-dependent ADH was present depending on the alcohol used as the carbon source. |