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

• Autorzy: Dabrowska A. , Szoltysik M. , Babij K. , Pokora M. , Zambrowicz A. , Chrzanowska J.
• Języki publikacji: EN

Abstrakty

EN

 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.

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2013
• Tom: 60
• Numer: 1
• Opis fizyczny: p.117-122,fig.,ref.

Twórcy

autor

Dabrowska A.

• Department of Animal Products Technology and Quality Management, Wrocław University of Environmental and Life Sciences, Wrocław, Poland

autor

Szoltysik M.

• Department of Animal Products Technology and Quality Management, Wrocław University of Environmental and Life Sciences, Wrocław, Poland

autor

Babij K.

• Department of Animal Products Technology and Quality Management, Wrocław University of Environmental and Life Sciences, Wrocław, Poland

autor

Pokora M.

• Department of Animal Products Technology and Quality Management, Wrocław University of Environmental and Life Sciences, Wrocław, Poland

autor

Zambrowicz A.

• Department of Animal Products Technology and Quality Management, Wrocław University of Environmental and Life Sciences, Wrocław, Poland

autor

Chrzanowska J.

• Department of Animal Products Technology and Quality Management, Wrocław University of Environmental and Life Sciences, Wrocław, Poland

Bibliografia

• Ardo Y, Gripon JC (1995) Comperative study of peptidolysis in some semi-chard round eyed cheese varieties with different fat contents. J Dairy Res 62: 543-547.
• Benzie IFF, Strain JJ (1996) Ferric reducing ability of plasma (FRAP) as a measure of antioxidant power: The FRAP assay. Anal Biochem 239: 70-76. 
• Bruno MA, Lazza CM, Errasti ME, Lopez LMI, Caffini NO, Pardo MF (2010) Milk clotting and proteolytic activity of an enzyme preperation from bromelia hieronimi fruits. Food Sci Tech 43: 695-701.
• Cervato G, Cazzola R, Cestaro B, (1999) Studies on the antioxidant activity of milk caseins. Int J Food Sci Nutr 50: 291-296. 
• Christensen TMIE, Kristiansen KR, Madsen JS (1989) Proteolysis in cheese investigated by high-performance liquid chromatography. J Dairy Res 56: 823-828.
• Czajgucka A, Szołtysik M, Juszczyk P, Żelazko M, Połomska X, Dąbrowska A, Wojtatowicz M, Chrzanowska J (2007) Yeast strains isolated from Rokpol cheese - their growth in milk and hydrolytic activity against milk components. Acta Sci Pol, Biotechnologia 6: 3-13 (in Polish).
• Dryjański M, Otlewski J, Polanowski A, Wilusz T (1990) Serine proteinase from Cucurbita ficifolia seed; purification, properties, substrate specificity and action on native squash trypsin inhibitor (CMTI I). Biol Chem Hoppe-Seyler 371: 889-895.  
• Flaczyk E, Kobus J, Rudzińska M, Buszka K, Górecka D, Szczepaniak B, Korczak J (2005) Evaluation of quality of "extra virgin" olive oils available in retail. Rośliny Oleiste - Oilseed Crops 26: 621-630.
• Haque E, Chand R (2008) Antihypertensive and antimicrobial bioactive peptides from milk proteins. Eur Food Res Technol 227: 7-15.
• Hekmat S , McMahon DJ (1998) Distribution of iron between caseins and whey proteins in acidified milk. Food Sci Technol 31: 632-638.
• Iwaniak A, Minkiewicz P (2007) Proteins as the source of physiologically and functionally active peptides. Acta Sci Pol, Technol Aliment 6: 5-15.
• Korhonen H, Pihlanto-Leppälä A (2001) Milk protein-derived bioactive peptides -novel opportunities for health promotion. IDF Bull 363: 17-26. 
• Korhonen H, Pihlanto-Leppälä A, Rantamäki P, Tupasela T (1998) Impact of processing on bioactive proteins and peptides. Trends Food Sci Technol 9: 307-319.
• Korhonen H, Pihlanto A (2006) Bioactive peptides: production and functionality. Int Dairy J 16: 1-15.
• Kuchroo CV, Ramilly IP, Fox PF (1983) Assesment of proteolysis in cheese by reaction with trinitrobenzosulfonic acid. J Food Technol 7: 129-133.
• Lahov E, Edelsten D, Sode-Morgensen MT, Sofer E (1971) Properties of basic glycopeptides released from cow milk protein by heat. Milchwissenschaft 26: 489-495.
• Lowry OH, Rosebrough J, Farr AL, Randall RJ (1951) Protein Measurement with the Folin Phenol Reagent. J Biol Chem 193: 265-275. 
• Meisel H (2004) Multifunctional peptides encrypted in milk proteins. BioFactors 21: 55-61. 
• Netto FM, Galeazzi AM (1998) Production and characterization of enzymatic hydrolysate from soy protein isolate. Lebensm Wiss Technol 31: 624-631.
• Parka PJ, Jung WK, Nam KS, Shahidi F, Kim SK (2001) Purification and characterization of antioxidative peptides from protein hydrolysate of lecithin-free egg yolk. J Amer Oil Chem Soc 78: 651-656.
• Pasupuleti M, Davoudi M, Malmsten M, Schmidtchen A (2009) Antimicrobial activity of a C-terminal peptide from human extracellular superoxide dismutase. BMC Res Notes 2: 136. 
• Pellegrini A, Thomas U, Bramaz N, Hunziker P, Fellenberg R (1999) Isolation and identification of three bactericidal domains in the bovine α-lactalbumin molecule. Biochim Biophys Acta 1426: 439-448. 
• Phelan M, Aherne-Bruce SA, O'Sullivan D, FitzGerald RJ, O'Brien NM (2009) Potential bioactive effects of casein hydrolysates on human cultured cells. Int Dairy J 19: 279-285.
• Pihlanto A (2006) Antioxidative peptides derived from milk proteins. Int Dairy J 16: 1306-1314.
• Pihlanto A, Korhonen H (2003) Bioactive peptides and proteins. Adv Food Nutr Res 47: 175-276. 
• Pralea D, Dumitrascu L, Borda D, Stanciuc N (2011) Functional properties of sodium caseinate hydrolases as affected by the extent of chymotrypsinolysis. J Agro Proc Tech 17: 308-314.
• Rival SG, Boeriu CG, Wichers HJ (2001) Caseins and casein hydrolysates. 2. Antioxidative properties and relevance to lipoxygenase inhibition. J Agric Food Chem 49: 295-302. 
• Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379. 
• Spellman D, McEvoy E, O'Cuinn G, FitzGerald RJ (2003) Proteinase and exopeptidase hydrolysis of whey protein: comparison of the TNBS, OPA and pH stat methods for quantification of degree of hydrolysis. Int Dairy J 13: 447-453.
• Suetsuna K, Ukeda H, Ochi H (2000) Isolation and characterization of free radical scavenging activities peptides derived from casein. J Nutr Biochem 11: 128-131. 
• Yen GC, Chen HY (1995) Antioxidant activity of various tea extracts in relation to their antimutagenicity. J Agric Food Chem 43: 27-32.
• Xu X, Katayama S, Mine Y (2007) Antioxidant activity of triptic digest of hen egg yolk phosvitin. J Sci Food Agic 87: 2604-260. 

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