Registration Dossier

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Please be aware that this old REACH registration data factsheet is no longer maintained; it remains frozen as of 19th May 2023.

The new ECHA CHEM database has been released by ECHA, and it now contains all REACH registration data. There are more details on the transition of ECHA's published data to ECHA CHEM here.

Diss Factsheets

Administrative data

Endpoint:
basic toxicokinetics in vitro / ex vivo
Type of information:
migrated information: read-across based on grouping of substances (category approach)
Adequacy of study:
supporting study
Study period:
1972
Reliability:
2 (reliable with restrictions)
Rationale for reliability incl. deficiencies:
other: The study is not following any official guideline, but scientifcally valid and useful to confirm a step of the metabolic pattern of fatty acid methyl esters

Data source

Reference
Reference Type:
publication
Title:
Hydrolysis of fully esterified alcohols containing from one to eight hydroxyl groups by the lipolytic enzymes of rat pancreatic juice
Author:
Mattson F.H.
Year:
1972
Bibliographic source:
Journal of Lipid Research Volume 13, 1972

Materials and methods

Objective of study:
metabolism
GLP compliance:
no

Test material

Constituent 1
Chemical structure
Reference substance name:
Methyl oleate
EC Number:
203-992-5
EC Name:
Methyl oleate
Cas Number:
112-62-9
Molecular formula:
C19H36O2
IUPAC Name:
Methyl (Z)-octadec-9-enoate

Results and discussion

Applicant's summary and conclusion

Conclusions:
Interpretation of results (migrated information): no bioaccumulation potential based on study results
Executive summary:

The enzymatic hydrolysis in vitro of the esters of methanol, ethylene glycol, glycerol, erythritol, pentaerythritol, adonitol, sorbitol, and sucrose in which the alcohol groups were esterified with oleic acid was studied. Various preparations of rat pancreatic juice, including pure lipase, were used as the sources of enzymes. Lipase (EC 3.1.1.3) did not hydrolyze compounds that contained more than three ester groups. Compounds containing four and five ester groups were hydrolyzed by certain preparations of pancreatic juice; this activity is attributed to the enzyme, nonspecific lipase. This enzyme also hydrolyzed esters of primary alcohols. The compounds containing six (sorbitol) and eight (sucrose) ester groups were not hydrolyzed