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Isoprotein composition and cross‐linking of thaumatins using mushroom tyrosinase and dimethyl suberimidate
Author(s) -
RAMSOHOYE PAMELA V.,
KOZLOV I. A.
Publication year - 1991
Publication title -
international journal of food science and technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.831
H-Index - 96
eISSN - 1365-2621
pISSN - 0950-5423
DOI - 10.1111/j.1365-2621.1991.tb01164.x
Subject(s) - thaumatin , chemistry , tyrosinase , dimer , sweetness , biochemistry , taste , mushroom , stereochemistry , food science , enzyme , organic chemistry , gene
Summary Analysis of commercial thaumatin has now provided some evidence for more than the six known isoproteins by further resolution of thaumatins 0 and II. Purified isolates of thaumatins I and II were modified by mushroom tyrosinase and dimethyl suberimidate, creating cross‐linked thaumatin oligomers. The dimer ( M r 44400–44600) from the tyrosinase reaction still retained some sweetness, but the other did not. This dimer is one of the largest molecules so far observed as having a sweet taste.