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Identification of Odoriferous Sulfanylalkanols in Human Axilla Secretions and Their Formation through Cleavage of Cysteine Precursors by a CS Lyase Isolated from Axilla bacteria
Author(s) -
Natsch Andreas,
Schmid Joachim,
Flachsmann Felix
Publication year - 2004
Publication title -
chemistry and biodiversity
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.427
H-Index - 70
eISSN - 1612-1880
pISSN - 1612-1872
DOI - 10.1002/cbdv.200490079
Subject(s) - cysteine , chemistry , enzyme , lyase , biochemistry , bacteria , recombinant dna , axilla , escherichia coli , odor , microbiology and biotechnology , gene , biology , organic chemistry , genetics , cancer , breast cancer
Human axillary odor is known to be formed upon the action of Corynebacteria sp. on per se odorless axilla secretions. Besides the known odoriferous acids, we report the occurrence in human axilla secretions of four odoriferous sulfanylalkanols, namely 3‐sulfanylhexan‐1‐ol ( 3 ), 2‐methyl‐3‐sulfanylbutan‐1‐ol ( 4 ), 3‐sulfanylpentan‐1‐ol ( 5 ), and 3‐methyl‐3‐sulfanylhexan‐1‐ol ( 6 ). These compounds have a pungent sweat/kitchen odor, also reminiscent of onions with some fruity connotations, and perception thresholds in the pg/l range. It was postulated that the odorless precursors for these compounds are cysteine conjugates. Bacterial isolates obtained from the human axilla and belonging to the Corynebacteria were, indeed, found to have the enzymatic capacity to release various thiols from cysteine conjugates. The met C gene, which is known to code for a cystathione‐ β ‐lyase, was cloned from the axilla isolate Corynebacterium striatum Ax20 and heterologously expressed in E. coli. The pure recombinant enzyme cleaves various cysteine conjugates and has a similar substrate specificity as the cell homogenates of the wild‐type. The recombinant enzyme was finally incubated with odorless axilla secretions and shown to release odoriferous thiols.