In Silico and In Vitro Assessment of Portuguese Oyster () Proteins as Precursor of Bioactive Peptides.

In this study, the potential bioactivities of Portuguese oyster () proteins were predicted through in silico analyses and confirmed by in vitro tests. proteins were characterized by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and identified by proteomics techniques. Hydrolysis simulation by BIOPEP-UWM database revealed that pepsin (pH > 2) can theoretically release greatest amount of bioactive peptides from proteins, predominantly angiotensin I-converting enzyme (ACE) and dipeptidyl peptidase IV (DPP-IV) inhibitory peptides, followed by stem bromelain and papain.

Bioactivities of enzymatic protein hydrolysates derived from .

protein isolates were enzymatically hydrolyzed using pepsin, bromelain, and thermolysin, with their molecular characteristics and bioactivities determined. Thermolysin hydrolysates exhibited the highest degree of hydrolysis (18.08% ± 1.

Prediction of Bioactive Peptides from Proteins Using Proteomic Techniques in Combination with Bioinformatics Analyses.

is one of the most nutritionally important microalgae with high protein content and can be a good source of potential bioactive peptides. In the current study, isolated proteins from were subjected to in silico analysis to predict potential peptides with biological activities. Molecular characteristics of proteins were analyzed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and proteomics techniques.

Development and characterisation of charcoal briquettes from water hyacinth (Eichhornia crassipes)-molasses blend.

Charcoal briquettes are inexpensive solid fuels made from carbonized biomass. The potential of converting water hyacinth (Eichhornia crassipes) charcoal into briquettes with molasses as binder was investigated in this study. Dried water hyacinth was carbonized at a temperature between 350°C to 500°C in a fabricated fine biomass carbonizer.