Autolysis and the endogenous proteinases characterised in beardless barb (Anematichthys apogon) muscle. (26th July 2021)

• Record Type: Journal Article
• Authors: Sripokar, Pakteera; Zhang, Yi; Simpson, Benjamin K.; Hansen, Egon Bech; Maneerat, Suppasil; Klomklao, Sappasith
• Is Part Of: International journal of food science & technology. Volume 56:Number 12(2021)
• Page Start: 6368
• Page End: 6375
• Publication Date: 2021-07-26
• Subjects: Autolysis -- degradation -- fermented fish paste -- proteinase; Food industry and trade -- Periodicals; 664
• DOI: 10.1111/ijfs.15262
• Languages: English
• ISSNs: 0950-5423

Abstract

Summary: 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. Abstract : Cathepsin is the predominant proteinase responsible for autolysis in beardless bard muscle.