• Proceedings of the Ginseng society Conference
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• 1984.09a
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• pp.257-275
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• 1984

Enzymatic browning is considered desirable in tea and tobacco processing but undesirable in many fruits processing at the present time. It is necessary to understand the nature of the enzyme, phenoloxidase, in order to control browning reactions, and extend its effects to formation of browning products as antioxidants in ginseng. Ginseng exhibits antioxidant activity when incorporated with turkey dark meat patties. The activity in red ginseng showed about two times stronger than white ginseng. One of the phenolic antioxidants from fresh, white and reprocessed white ginseng was identified as phenol 2.6 Bis(1.1 dimethyl ethyl) 4-methyl among several unknown compounds by GC/mass spectrometer. In red ginseng, no phenol 2.6 Bis (1.1 dimethyl ethyl) 4-methyl was detected, the compound may be polymerized by phenoloxidase and form some higher molecular compounds which may possess high antioxidant activity. Phenoloxidase isozymes in fresh Korean ginseng (panax ginseng C.A. Meyer) were extracted with phosphate buffer at pH 7.3. The isozymes were purified through ammonium sulfate fractionation, dialysis and chromatography on a DEAE-cellulose column. Two groups of phenoloxidase were shown to be present, one in the floating agglomerated group and the other in the precipitate. group from the 0.85 saturation ammonium sulfate. The DEAE-cellulose column chromatography, the phenoloxidase isozyme present in the precipitate appears as the first peak (I), and that in the agglomerate in the second peak (II). Isozyme I showed higher activity with catechin and catechal, and isozyme II showed higher activity with p-cresol. The isozyme showed two optimum pH activity one at pH 4.5 and the other at 8.5 with catechin as substrate. Korean ginseng phenoloxidase has high heat stability. When heated at $75^{\circ}C$ for 2 hours, its activity remained $90\%\;and\;80\%$ on phenoloxidase I and II respectively. Phenoloxidase I was most active on (+) catechin followed by p-cresal, catechol and epicatechin. Phenoloxidase II was most active on p-cresal followed by (+) catechin, catechol, p-coumanic acid and epicatechin. Sodium bisulfite, sodium cyanide, ascorbic acid glutachion in the oxidized form, sodium diethyl dithiocarbomate and ethylendiamine tetra acetate (EDTA) acted as inhibitors. Red ginseng color development was initiated by phenoloxidase and finished by a followed sun drying process. The antiaging activity of ginseng may be initiated by the antioxidant in the ginseng.

• Korean Journal of Poultry Science
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• v.51 no.1
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• pp.1-9
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• 2024

To reduce salt content and enhance calcium in chicken patty, shell calcium powder (SCP) was added, and transglutaminase (TG) was included to improve its properties. Five different treatments were prepared to assess the effects: CON (2% salt), T1 (0.75% salt + 0.2% SCP), T2 (0.75% salt + 0.2% SCP + 0.2% TG), T3 (0.5% salt + 0.4% SCP), and T4 (0.5% salt + 0.4% SCP + 0.2% TG). Reducing salt led to decreased ash content and increased cooking loss. The addition of SCP and TG raised pH levels. Meat color remained consistent with different salt, SCP, and TG levels. However, when salt was reduced to 0.5% and SCP was added at 0.4% without TG, the patty's hardness and chewiness decreased. Sensory evaluations showed reduced juiciness when salt was reduced to 0.5% and SCP was added at 0.4%, but no significant differences were observed in overall acceptability. Salt had no impact on TBARS results, but salt reduction to below 0.5% increased susceptibility to microbial contamination. In summary, reducing salt and adding SCP had minimal sensory impact, but when salt is reduced to 0.5% or lower, consider adding TG. Also, when decreasing salt, additional preservatives should be considered to address potential microbial contamination during manufacturing.