Project description:Saccharomonospora azurea Runmao et al. 1987 is a member of the genus Saccharomonospora, which is in the family Pseudonocardiaceae and thus far poorly characterized genomically. Members of the genus Saccharomonospora are of interest because they originate from diverse habitats, such as leaf litter, manure, compost, the surface of peat, and moist and over-heated grain, and may play a role in the primary degradation of plant material by attacking hemicellulose. Next to S. viridis, S. azurea is only the second member in the genus Saccharomonospora for which a completely sequenced type strain genome will be published. Here we describe the features of this organism, together with the complete genome sequence with project status 'Improved high quality draft', and the annotation. The 4,763,832 bp long chromosome with its 4,472 protein-coding and 58 RNA genes was sequenced as part of the DOE funded Community Sequencing Program (CSP) 2010 at the Joint Genome Institute (JGI).
Project description:BackgroundFish byproducts are commonly recognized as low-value resources. In order to increase the value, fish byproducts need to be converted into new products with high functionality such as fish protein hydrolysate (FPH). In this study, FPH manufactured from parrotfish (Chlorurus sordidus) heads using different pH, time and sample ratio was investigated.MethodsHydrolysis reactions were conducted under different pHs (5, 7, and 9) and over different durations (12 and 24 h). Control treatment (without pH adjustment (pH 6.4)) and 0 h hydrolsisis duration were applied. Hydrolysates were characterized with respect to proximate composition, amino acid profile, and molecular weight distribution. The antioxidant activity of the hydrolysate was also observed.ResultsThe pH and duration of hydrolysis significantly affected (p < 0.05) the characteristics of FPH. The highest yield of hydrolysate (49.04 ± 0.90%), with a degree of hydrolysis of 30.65 ± 1.82%, was obtained at pH 9 after 24 h incubation. In addition, the FPH had high antioxidant activity (58.20 ± 0.55%), with a high level of essential amino acids. Results suggested that FPH produced using endogenous enzymes represents a promising additive for food and industrial applications.