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Application of Asian pumpkin (Cucurbita ficifolia) serine proteinase for production of biologically active peptides from casein

100%

Dąbrowska A., Szołtysik M., Babij K., Pokora M., Zambrowicz A., Chrzanowska J.

Acta Biochimica Polonica

2013

vol. 60

issue 1

117-122

The main objective of this study was to determine potential application of a serine proteinase derived from Asian pumpkin for obtaining biologically active peptides from casein. The course of casein hydrolysis by three doses of the enzyme (50, 150, 300 U/mg of protein) was monitored for 24 hours by the determinations of: hydrolysis degree DH (%), free amino group content (μmole Gly/g), RP HPLC peptide profiles and by polyacrylamide gel electrophoresis. In all hydrolyzates analyzed antioxidant activities were determined using three tests: the ability to reduce iron ions in FRAP test, the ability to scavenge free radicals in DPPH test, and Fe2+ chelating activity. The antimicrobial activity of obtained peptide fractions was determined as the ability to inhibit the growth of Escherichia coli, Bacillus cereus and Pseudomonas fluorescens in a diffusion plate test. The deepest degradation, expressed as the DH [%] and the free amino group content (67% and 7528 µmole Gly/mg, respectively), was noted in samples hydrolyzed with 300 U/ml of enzyme for 24 hours, while in other samples the determined values were about three and two times lower. The results were in agreement with the peptide profiles obtained by RP HPLC. The highest antioxidative activities determined in all tests were seen for the casein hydrolysate obtained with 300 U/mg protein of serine proteinase after 24 h of reaction (2.15 µM Trolox/mg, 96.15 µg Fe3+/mg, 814.97 µg Fe2+/mg). Antimicrobial activity was presented in three preparations. In other samples no antimicrobial activity was detected.

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.

Acta Biochimica Polonica

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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2 Acta Biochimica Polonica

1 2017

1 2013

2 Babij K.

2 Chrzanowska J.

2 Dąbrowska A.

2 Pokora M.

2 Szołtysik M.

2 Zambrowicz A.

1 Eckert E.

1 Trziszka T.

1 Zabłocka A.

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Application of Asian pumpkin (Cucurbita ficifolia) serine proteinase for production of biologically active peptides from casein

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