Preservation of fish by embedment in Sphagnum moss,
peat, or holocellulose:
experimental proof of the oxopolysaccharidic nature
of the preservative substance and its antimicrobial and tanning action.
Børsheim, Knut Yngve, Bjørn Erik Christensen, and
Terence J. Painter (2001)
Innovative Food Science and Emerging Technologies
2:63-74
Abstract
Strips of salmon (Salmo
salar) skin or whole zebra fish (Brachydanio rerio) were preserved
for many weeks by embedment in untreated Sphagnum palustre moss (A),
peat derived mainly from Sphagnum mosses (B), acetone - extracted moss
(C), or the chlorite holocellulose of the moss (D). Preservation occurred in
the presence of oxygen at 20 - 23°C, and between pH 3.4 - 5.1. Product D, which
was a pure, insoluble, white polysaccharide, performed as well or better than
the other materials. It contained ~0.5 mmole·g-1 of highly reactive
carbonyl groups, and when these were removed by borohydride reduction or
condensation with ammonia, the preservative property was lost. Preservation was
invariably accompanied by a browning of the dermis and a yellowing of the
scales, and was attributed to a Maillard reaction since neither occurred when
the carbonyl groups were removed.
A water-soluble fragment (‘sphagnan’)
of D, containing 1.0 mmole·g-1 of carbonyl groups, had an astringent
taste in aqueous solution and produced effects similar to those brought about
by embedment in A, B, C or D, albeit more rapidly. Films of mackerel (Scomber
scombrus) skin became brown and completely bio-resistant after repeated
immersion in aqueous (3% w/v) sphagnan with intermittent drying, whereas
similar treatment with borohydride-reduced sphagnan had no effect. Differential
thermal analysis (DSC) of the sphagnan-treated skin gave results consistent
with tanning by covalent cross-linking. Hence the chemical and visible colour
changes associated with embedment in the moss products or immersion in aqueous
sphagnan resemble those brought about by exposure to wood smoke. Filleted fish muscle
cannot, however, be preserved in these ways because soluble protein diffuses
out from the muscle too quickly, and neutralizes the carbonyl groups
selectively.