Abstract
The formation of lysinoalanine (LAL) in protein recovered from the belanger's croaker, Johnius grypotus, using a pH shifting process was measured by amino acid analysis. The LAL peak was detected at 49.24 min, between phenylalanine and histidine peaks in the amino acid analyzer. LAL was not detected in the fish muscle or in protein recovered using the alkaline pH shifting process. LAL was not formed in protein recovered after storage for up to 9 hrs at pH 11, but was detected in the soluble protein fraction at pH 11, followed heating at <TEX>$90\;^{\circ}C$</TEX>. The myosin heavy chain decreased with storage time at pH 11. The results suggest that the alkaline shifting process for recovering fish muscle protein is safe, and that no LAL forms.
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