Ferrochelatase catalyzes the formation of Zn-protoporphyrin of dry-cured ham via the conversion reaction from heme in meat.

Ferrochelatase (FECH), the enzyme at the last step of the heme-biosynthetic pathway, is involved in the formation of Zn-protoporphyrin via an iron-removal reaction of heme. To improve the efficacy of the formation of Zn-protoporphyrin from heme, the use of recombinant FECHs from porcine, yeast, and bacteria was examined. Incubation of FECH with myoglobin in the presence of ascorbic acid and cysteine resulted in the efficient conversion of myoglobin-heme to Zn-protoporphyrin. Exogenously added recombinant yeast FECH facilitates the production of Zn-protoporphyrin from myoglobin-heme and heme in meat, via the replacement of iron in the protoporphyrin ring by zinc ions. A large amount of Zn-protoporphyrin was also generated by the catalysis of FECH using an intact piece of meat as a substrate. These findings can open up possible approaches for the generation of a nontoxic bright pigment, Zn-protoporphyrin, to shorten the incubation time required to produce dry-cured ham.