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Autolysis and the endogenous proteinases characterised in beardless barb (Anematichthys apogon) muscle |
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| Authors: | Pakteera Sripokar Yi Zhang Benjamin K Simpson Egon Bech Hansen Suppasil Maneerat Sappasith Klomklao |
| Affiliation: | 1. Biotechnology Program, Faculty of Agro and Bio Industry, Thaksin University, Phatthalung Campus, Phatthalung, 93210 Thailand
Contribution: Data curation (lead), Methodology (lead), Writing - original draft (lead);2. Department of Food Science & Agricultural Chemistry, McGill University, 21111 Lakeshore Road, Ste-Anne-de-Bellevue, Montreal, QC, H9X 3V9 Canada IPREM, CNRS, Université de Pau et des Pays de l’Adour, Pau, E2S UPPA 64000 France Contribution: Supervision (equal), Writing - review & editing (supporting);3. Department of Food Science & Agricultural Chemistry, McGill University, 21111 Lakeshore Road, Ste-Anne-de-Bellevue, Montreal, QC, H9X 3V9 Canada Contribution: Supervision (equal);4. Technical University of Denmark, National Food Institute, Kgs. Lyngby, 2800 Denmark;5. Department of Industrial Biotechnology, Faculty of Agro-Industry, Prince of Songkla University, Hat Yai, Songkhla, 90112 Thailand Contribution: Software (equal), Validation (equal);6. Department of Food Science and Technology, Faculty of Agro and Bio Industry, Thaksin University, Phatthalung Campus, Phatthalung, 93210 Thailand |
| Abstract: | Beardless barb is a common fish species used in fermentation of fish paste Ka-pi-plaa. Autolytic profile of beardless barb muscle showed the maximum autolysis was at 50 °C, at both acidic and alkaline pH values. With augmentation concentration of NaCl, autolytic activity slightly decreased. Endogenous proteinases isolated from fish muscle in crude extract forms were also characterised. The acidic proteinases had optimum activity at pH 3.0 and 50°C, and they showed higher proteolytic activity than the alkaline proteinases which were optimally active at pH 9.0 and 50 °C. Proteinases in peak at pH 3.0 were inhibited by pepstatin A, but those in peak at pH 9.0 were highly inhibited by PMSF, TLCK and soybean trypsin inhibitor, suggesting that both aspartic and serine proteinases were existed in beardless barb muscle. The proteinases were stable in pH range of 2.0-5.0 but unstable at the temperatures higher than 40 °C. NaCl suppressed the proteolytic activity, ATP activated the proteinase activity, while CaCl2, MgCl2 and CoCl2 exhibited no influence on the activity. The results implied that cathepsin D is the predominant proteinase responsible for autolysis in beardless barb. The findings were useful to improve the processing and qualities of Ka-pi-plaa product using beardless barb as raw material. |
| Keywords: | Autolysis degradation fermented fish paste proteinase |