Quality of Protein Isolates and Hydrolysates from Baltic Herring (Clupea harengus membras) and Roach (Rutilus rutilus) Produced by pH-Shift Processes and Enzymatic Hydrolysis

Fractionation is a potential way to valorize under-utilized fishes, but the quality of the resulting fractions is crucial in terms of their applicability. The aim of this work was to study the quality of protein isolates and hydrolysates extracted from roach (Rutilus rutilus) and Baltic herring (Clupea harengus membras) using either pH shift or enzymatic hydrolysis. The amino acid composition of protein isolates and hydrolysates mostly complied with the nutritional requirements for adults, but protein isolates produced using pH shift showed higher essential to non-essential amino acid ratios compared with enzymatically produced hydrolysates, 0.84–0.85 vs. 0.65–0.70, respectively. Enzymatically produced protein hydrolysates had a lower total lipid content, lower proportion of phospholipids, and exhibited lower degrees of protein and lipid oxidation compared with pH-shift-produced isolates. These findings suggest enzymatic hydrolysis to be more promising from a lipid oxidation perspective while the pH-shift method ranked higher from a nutrient perspective. However, due to the different applications of protein isolates and hydrolysates produced using pH shift or enzymatic hydrolysis, respectively, the further optimization of both studied methods is recommended.

Determination of the Metastable Zone Width and Nucleation Parameters of Succinic Acid for Electrochemically Induced Crystallization

Electrified downstream processes for biotechnologically produced carboxylic acids reduce waste salt generation significantly and make biotechnological production ecologically and economically more attractive. In order to design, optimize, scale-up and control electrochemically induced crystallization processes, knowledge of the metastable zone width (MSZW) is essential. An optical observation approach of nucleation processes close to the electrode and determination of the MSZW is presented. This work presents a method for MSZW measurements for electrochemically induced pH-shift crystallization processes by monitoring the nucleation, the saturation pH value and saturation concentration for different current densities. The measured MSZWs for electrochemically induced pH-shift crystallization are narrow due to the foreign surface, gas bubbles and electrode surface, and rising current densities lead to even smaller MSZW. Nucleation parameters are estimated from MSWZ data, adapting the classical approach of Nývlt to electrochemically induced crystallization.

Characterisation of pH-shift-produced protein isolates from sago palm weevil (Rhynchophorus ferrugineus) larvae

Farm-raised sago palm weevil (Rhynchophorus ferrugineus) larvae (SPWL) can be used as a protein source for food sustainability. This study aimed to investigate the potential of pH-shift processing as a cold refinery approach to produce protein isolate from SPWL. Maximum solubility of SPWL protein was observed at pH 2.0 (acid-aided process) and pH 11.5 (alkaline-aided process). The zeta-potential of the protein solution was close to zero with the lowest solubility at pH 4.5. So, the protein precipitation was performed at this pH. Although both acid and alkaline methods yielded roughly 66% protein, their nutritional and techno-functional features differed based on the pH-shifting process. The alkaline-produced protein isolate had higher essential amino acid (EAA) content and EAA index but it was darker in colour. The acid-produced protein isolate had larger levels of umami-taste-active and functional amino acids, as well as a higher emulsifying capability.

Partial Removal of Phenolics Coupled with Alkaline pH Shift Improves Canola Protein Interfacial Properties and Emulsion in In Vitro Digestibility

The effect of polyphenol removal (“dephenol”) combined with an alkaline pH shift treatment on the O/W interfacial and emulsifying properties of canola seed protein isolate (CPI) was investigated. Canola seed flour was subjected to solvent extraction to remove phenolic compounds, from which prepared CPI was exposed to a pH12 shift to modify the protein structure. Dephenoled CPI had a light color when compared with an intense dark color for the control CPI. Up to 53% of phenolics were removed from the CPI after the extraction with 70% ethanol. Dephenoled CPI showed a partially unfolded structure and increased surface hydrophobicity and solubility. The particle size increased slightly, indicating that soluble protein aggregates formed after the phenol removal. The pH12 shift induced further unfolding and decreased protein particle size. Dephenoled CPI had a reduced β subunit content but an enrichment of disulfide-linked oligopeptides. Dephenol improved the interfacial rheology and emulsifying properties of CPI. Although phenol removal did not promote peptic digestion and lipolysis, it facilitated tryptic disruption of the emulsion particles due to enhanced proteolysis. In summary, dephenol accentuated the effect of the pH shift to improve the overall emulsifying properties of CPI and emulsion in in vitro digestion.