Nanofibrillated cellulose (NFC) gels simultaneously exhibiting Pickering stabilizing capability and thermally stable green color were developed for use as food additive in thermally processed food emulsion requiring the expression of color. Chopped Centella asiatica plant was mixed with zinc amino acid chelate solution and subject to autoclaving at 130°C for 2 h to form zinc‐chlorophylls complex and to remove noncellulosic components. Autoclaved sample was high‐shear homogenized at 26,000 rpm for 15 min and microfluidized at either 80, 120, or 160 MPa for 5 passes. An increase in microfluidization pressure resulted in a decrease in NFC diameters; microfluidization at 160 MPa did not nevertheless yield any further reduction in the diameters when compared with that at 120 MPa. From energy consumption point of view, microfluidization at 120 MPa for 5 passes was then noted as optimal condition for preparation of NFC coloring gel; NFC with diameters of 8–42 nm and crystallinity index of 35% was obtained. Freshly prepared gel exhibited gel‐like behavior and dark green color. Heating at 121°C for 1 h did not affect diameters, viscoelasticity, and color of the gel. Addition of the gel at 0.9% or 1.2% (w/w) into soybean oil‐in‐water emulsion, in combination with high‐shear homogenization at 18,000 rpm for 5 min, resulted in adequate emulsion stability. The emulsion exhibited stable dark green color and no phase separation after heating at 121°C for 1 h and during storage for 8 weeks. Practical Applications Information presented here can serve as a guideline for further development of a multifunctional food ingredient exhibiting thermally stable green color and oil‐in‐water emulsion stabilizing capability. In other words, one simple ingredient can serve at the same time as both natural food colorant and emulsion stabilizer.
Clown featherback (Chitala ornata) is a freshwater fish important in the cuisine of Thailand and other Southeast Asian countries. It has a short marketable life due mainly to poor gelling characteristic even when stored in ice. This deterioration has been associated with muscle autolysis. The research was aimed to investigate the autolysis of clown featherback muscle (CFM). To test autolysis, mince from CFM was incubated in atemperature controlled water bath for 60 min at 5, 10, 20, 30, 40, 50, 60, 65, 70, 75 or 80 °C at pH levels over the range of 2-11. The results showed that the highest autolytic activity was at 70 ºC and it occurred at pH levels of 4 and 7, with pH 4 showing the highest autolysis. A (20.3% inhibition), which had significantly higher inhibitory activity (P<0.05) among the protease inhibitors tested. This suggests that aspartic protease was the major proteinase in CFM. CFM was incubated with its crude enzyme counterpart at the physiological pH (6.73) at both 4 ºC and 25 ºC. Degradation of natural actomyosin showed that after incubation at either temperature myosin heavy chain was susceptible to hydrolysis indicating that autolysis of CFM took place even at low temperature as affected by its endogenous proteases. The effects of several protease inhibitors were tested and autolysis at the physiological pH (6.73) was strongly inhibited by 10 µM pepstatin
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