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

100%

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

Acta Biochimica Polonica

2017

tom 64

nr 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.

Aktywnosc dehydrogenazy izocytrynianowej drozdzy a tempo tworzenia kwasu cytrynowego

86%

Robak M. , Wojtatowicz M. , Rymowicz W.

Zeszyty Naukowe Akademii Rolniczej we Wrocławiu. Technologia Żywności

1996

tom 10

27-35

Charakterystyka biomasy drozdzy Yarrowia lipolytica wyprodukowanej na substratach tluszczowych

72%

Rymowicz W. , Kinal S. , Musial I. , Bodarski R.

nr 3

70-77