The acid and alkaline solubilization processes for isolating muscle protein from ground fish raw materials are investigated by scrutinizing the literature. Following an introduction to the processes, with some underlying chemistry, patents related to the acid and alkaline solubilization process are described together with previously patented methods for processing of protein isolates. Focus is then placed on comparing a range of factors important in fish muscle protein isolation between the acid and alkaline solubilization processes, and classic washing-based surimi technology. The factors addressed were: protein yield, gel quality, color, lipid reduction, lipid oxidation, microbial stability, and frozen storage stability. A long series of studies made with different fish/shellfish species have been used for this purpose. Certain results are summarized in table form (protein yields, gel strength, and whiteness), others only in text form. From this part of the review, it is obvious that the acid process often has certain advantages (e.g., protein yield) and the alkaline process other ones (gel strength, whiteness, lipid removal, lipid oxidation, and total microbial count). Thus, the choice of method depends on the application. It is clear that most species respond differently to acid and alkaline solubilization, which is why the two methods are initially compared. In a section about new processing attempts, the use of the acid and alkaline methodology for isolating proteins from whole fish/shellfish and fish by-products is reviewed together with attempts to recover waste water proteins and attempts to modify the process. Tentative uses of the new protein isolates, e.g., as coatings, protein brines, and emulsifiers are finally described together with some conclusions and future opportunities for the acid and alkaline processes.

Filtration and centrifugation for separating functional proteins from an alkaline solubilisation process are investigated. The influence of the method of separation on the yield and the gel quality of surimi produced from the protein isolates was studied. The possibility of replacing centrifugation by filtration is investigated for a first and a second centrifugation step where the first centrifugation separates a dissolved protein phase at high pH from undissolved material and the second centrifugation separates precipitated proteins from the waterphase at neutral pH. The separation method greatly affects the yield and the quality of the processed surimi. Replacing the first centrifugation with sieving improves the yield of protein isolate, but worsens the quality of the produced gel. Replacing the second centrifugation with filtration has no influence on the yield or the quality of the protein isolate.

Previous studies of the pH-shift protein isolation process have shown that substantial amounts of solubilized proteins can be trapped in the sediments formed in the first centrifugation step of this process. As a strategy to improve the protein yield during pH-shift processing, the aim of this study was to evaluate how filtration as an alternative to centrifugation in the first separation step of pH-shift processing of blue whiting affected proteins yield and protein isolate characteristics (basic composition, polypeptide profiles, surimi gel quality and color attributes). The study comprised both the acid and alkaline versions of the method, and also fresh as well as frozen fish raw material. Results showed that the replacement of centrifugation with filtration substantially improved the protein yield by from about 38% to 62%, but also reduced the removal of lipid. There were no significant effects on gel quality. Protein isolates from fresh raw material were about 5 % whiter and frozen raw materials about 3% whiter with centrifugation as compared to filtration in the pHshift process. For surimi from fresh raw material centrifugation gave about 2 % whiter gels, while the gels from frozen raw material were about 3% whiter for filtered compared to centrifuged material. The whitest isolates and gels were obtained with acid processing of fresh blue whiting. Slight proteolytic breakdown resulting in fragments of 83 and 152 kDa was however noted with the acid process, especially when centrifugation was used.