Suchergebnisse

Seaweed represents an abundant, renewable, and fast-growing biomass resource for 3rd generation biofuel production. This study reports an efficient butanol fermentation process carried out by Clostridium beijerinckii DSM-6422 using enzymatic hydrolysate of the sugar-rich brown seaweed Laminaria digitata harvested from the coast of the Danish North Sea as substrate. The highest butanol yield (0.42 g/gconsumed-substrates) compared to literature was achieved, with a significantly higher butanol: acetone-butanol-ethanol (ABE) molar ratio (0.85) than typical (0.6). This demonstrates the possibility of using the seaweed L. digitata as a potential biomass for butanol production. For the first time, consumption of alginate components was observed by C. beijerinckii DSM-6422. The efficient utilization of sugars and lactic acid further highlighted the potential of using this strain for future development of large-scale cost-effective butanol production based on (ensiled) seaweed.

Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of Scyliorhinus canicula discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of pH and temperature on the hydrolysis of the S. canicula muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8°C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The pH optimum and temperature optimum for antioxidants were 55 ° C/pH8.0 for ABTS/DPPH-Esperase, 63.1 ° C/pH9.0 for DPPH-Alcalase, and 55° C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex. ; Fil: Vázquez, José A. Consejo Superior de Investigaciones Científicas; España ; Fil: Blanco, Maria. Consejo Superior de Investigaciones Científicas; España ; Fil: Massa, Agueda Elena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Mar del Plata. Instituto de Investigaciones Marinas y Costeras. Subsede Instituto Nacional de Investigación y Desarrollo Pesquero; Argentina ; Fil: Amado, Isabel Rodríguez. Universidad de Vigo; España ; Fil: Pérez Martín, Ricardo I. Consejo Superior de Investigaciones Científicas; España

The interest in collagen use in the food industry to replace synthetic agents is growing every day. Among the derivatives, has the hydrolysate, which dissolves easily in water and brine, and can be incorporated into foods or drinks. The objective of this study was to determine the degree of hydrolysis (DH) of crude collagen fiber, powdered collagen fiber, gelatin and two samples of hydrolyzed collagen. The substrates were subjected to individual action of three proteolytic enzymes: papain, bromelain and collagenase (microbial origin). The substrates were incubated in sodium phosphate buffer (0.1 M, pH 7.0) on an orbital shaker at 55°C for different periods of time. In 120 minutes of hydrolysis, the crude collagen fiber showed 37.2% of DH using collagenase, the highest value compared to other substrates. The lowest values for DH were obtained for the hydrolysates collagen, with less than 1% of DH. For hydrolysis in 60 minutes, the DH values were similar to those obtained in 120 minutes of hydrolysis, with minor variations over time. The hydrolytic ability of the collagenase and bromelain was similar and superior compared with the papain.

Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of Scyliorhinus canicula discards, which might account for up to 90–100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of pH and temperature on the hydrolysis of the S. canicula muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8 °C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The pH optimum and temperature optimum for antioxidants were 55 °C/pH8.0 for ABTS/DPPH-Esperase, 63.1 °C/pH9.0 for DPPH-Alcalase, and 55 °C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.