A5038108037- Protein Hydrolysis and Bioactive Peptides
- Aquaculture Nutrition and Growth
- Algal biology and biofuel production
- Enzyme Production and Characterization
- Biochemical effects in animals
- Redox biology and oxidative stress
- Cassava research and cyanide
- Free Radicals and Antioxidants
- Insect Utilization and Effects
- Animal Genetics and Reproduction
- Agriculture and Rural Development Research
- Enzyme Catalysis and Immobilization
- Food Science and Nutritional Studies
Central South University
2021-2024
Crude enzymes produced by a marine bacterium Pseudoalteromonas sp. JS4-1 were used to hydrolyze phycobiliprotein. Enzymatic productions showed good performance on DPPH radical and hydroxyl scavenging activities (45.14 ± 0.43% 65.11 2.64%, respectively), especially small peptides with MWCO <3 kDa. Small fractioned four fractions using size-exclusion chromatography the second fraction (F2) had highest activity in ability (62.61 5.80%). The F1 F2 both exhibited antioxidant oxidative stress...
Mesonia algae K4-1 from the Arctic secretes a novel cold-adapted and salt-tolerant protease EK4-1. It has highest sequence similarity with Stearolysin, an M4 family Geobacillus stearothermophilus, only 45% identity, is protease. Ek4-1 low optimal catalytic temperature (40 °C) stable at temperatures. Moreover, EK4-1 still active in 4 mol/L NaCl solution tolerant to surfactants, oxidizing agents organic solvents; furthermore, it prefers hydrolysis of peptide bonds P1' position as hydrophobic...
In the current study, microalgae Chlorella protothecoides (FACHB-2) was hydrolyzed by several kinds of extracellular bacterial proteases produced Pseudoalteromonas sp. ZB23-2, B27-3 and JS4-1 with subsequent extraction lipids performed using fewer toxic solvents. Through enzymatic hydrolysis, hydrolysates high antioxidant activity were obtained: DPPH radical, hydroxyl free hydrogen peroxide radical scavenging activities reached 33.47 ± 0.68%, 46.81 2.38%, 7.35 0.37 µmol·TE/µmol respectively....
Crude enzymes produced by a marine bacterium Pseudoalteromonas sp. JS4-1 were used to hydrolyze phycobiliprotein. Enzymatic productions showed good performance on DPPH radical and hydroxyl scavenging activities (45.14±0.43% 65.11±2.64%, respectively), especially small peptides with MWCO <3 kDa. Small fractioned four fractions using size-exclusion chromatography the second fraction (F2) had highest activity in ability (62.61±5.80%). The F1 F2 both exhibited antioxidant oxidative stress models...