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Production of calcium preparations by technology of saltwater fish by product processing

100%

Bubel F., Dobrzański Z., Bykowski P. J., Chojnacka K., Opaliński S., Trziszka T.

Open Chemistry

2015

vol. 13

issue 1

The paper presents the technology of processing Baltic cod (Gadus morhua callarias) and Atlantic salmon (Salmo salar) backbones – by-products from fish processing – for the production of calcium preparations. The raw material for the process consisted of backbones with remaining muscle tissue, devoid of heads and fins (30 kg of each type of backbones). The processing included the following stages: cutting, preliminary processing in an alkaline environment (soaking in 2 M NaOH), processing with 0.1% citric acid, aroma removal and material disinfection (5% H2O2), rinsing with tap water, drying, and grinding the end-product. Calcium preparations from cod (BCP) and salmon (ASP) in the amounts of 1.20 kg and 1.62 kg, respectively, characterized by high calcium content (27.79% in BCP, and 24.92% in ASP) and low protein and fat content (14.20% and 0.25% for BCP, and 10.78% and 0.12% for ASP, respectively) were obtained. The study demonstrated the effectiveness of this technology for production of calcium preparations from fish backbones.

The use of serine protease from Yarrowia lipolytica yeast in the production of biopeptides from denatured egg white proteins

84%

Pokora M., Zambrowicz A., Zabłocka A., Dąbrowska A., Szołtysik M., Babij K., Eckert E., Trziszka T., Chrzanowska J.

2017

vol. 64

issue 2

245-253

Deriving non-conventional enzymes from cheaper sources than those used for commercially available enzymes may result in the production of hydrolysates with beneficial features, while drastically reducing the cost of hydrolysis. This is especially significant for enzymatic hydrolysis as a method of protein waste utilization. We have previously described the ability of non-commercial serine protease from Yarrowia lipolytica yeast to produce/release bioactive peptides from egg white protein by-products (EP). The enzymatic hydrolysis of EP was carried out for 24 h using the serine protease at an enzyme: substrate ratio of 1:30 (w/w). The obtained hydrolysate was characterized by protein degradation of 38% and also exhibited an antioxidant and cytokine-inducing activity. The isolation procedure (ultrafiltration and RP-HPLC) of bioactive peptides from the EP hydrolysate provided peptide fractions with significant antioxidant and ACE inhibitory activities. Three homogeneous and three heterogeneous peptide fractions were identified using MALDI-TOF/MS and the Mascot Search Results database. The peptides, mainly derived from ovalbumin, were composed of 2-19 amino-acid residues. We have thus demonstrated a novel ability of serine protease from Y. lipolytica to release biopeptides from an EP by-product.

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1 Acta Biochimica Polonica

1 Open Chemistry

1 2017

1 2015

2 Trziszka T.

1 Babij K.

1 Bubel F.

1 Bykowski P. J.

1 Chojnacka K.

1 Chrzanowska J.

1 Dobrzański Z.

1 Dąbrowska A.

1 Eckert E.

1 Opaliński S.

1 Pokora M.

1 Szołtysik M.

1 Zabłocka A.

1 Zambrowicz A.

Search results

Production of calcium preparations by technology of saltwater fish by product processing

The use of serine protease from Yarrowia lipolytica yeast in the production of biopeptides from denatured egg white proteins