Search results for: Ž. Vaštag
2 Bioactivity Evaluation of Cucurbitin Derived Enzymatic Hydrolysates
Authors: Ž. Vaštag, Lj. Popović, S. Popović
Abstract:
After cold pressing of pumpkin oil, the defatted oil cake (PUOC) was utilised as raw material for processing of bio-functional hydrolysates. In this study, the in vitro bioactivity of an alcalase (AH) and a pepsin hydrolysate (PH) prepared from the major pumpkin 12S globulin (cucurbitin) are compared. The hydrolysates were produced at optimum reaction conditions (temperature, pH) for the enzymes, during 60min. The bioactivity testing included antioxidant and angiotensin I converting enzyme inhibitory activity assays. The hydrolysates showed high potential as natural antioxidants and possibly antihypertensive agents in functional food or nutraceuticals. Additionally, preliminary studies have shown that both hydrolysates could exhibit modest α-amylase inhibitory activity, which indicates on their hypoglycemic potential.
Keywords: Cucurbitin, alcalase, pepsin, protein hydrolysates, in vitro bioactivity.
Procedia APA BibTeX Chicago EndNote Harvard JSON MLA RIS XML ISO 690 PDF Downloads 25711 Hydrolysis of Hull-Less Pumpkin Oil Cake Protein Isolate by Pepsin
Authors: Ivan Živanović, Žužana Vaštag, Senka Popović, Ljiljana Popović, Draginja Peričin
Abstract:
The present work represents an investigation of the hydrolysis of hull-less pumpkin (Cucurbita Pepo L.) oil cake protein isolate (PuOC PI) by pepsin. To examine the effectiveness and suitability of pepsin towards PuOC PI the kinetic parameters for pepsin on PuOC PI were determined and then, the hydrolysis process was studied using Response Surface Methodology (RSM). The hydrolysis was carried out at temperature of 30°C and pH 3.00. Time and initial enzyme/substrate ratio (E/S) at three levels were selected as the independent parameters. The degree of hydrolysis, DH, was mesuared after 20, 30 and 40 minutes, at initial E/S of 0.7, 1 and 1.3 mA/mg proteins. Since the proposed second-order polynomial model showed good fit with the experimental data (R2 = 0.9822), the obtained mathematical model could be used for monitoring the hydrolysis of PuOC PI by pepsin, under studied experimental conditions, varying the time and initial E/S. To achieve the highest value of DH (39.13 %), the obtained optimum conditions for time and initial E/S were 30 min and 1.024 mA/mg proteins.Keywords: Enzymatic hydrolysis, Pepsin, Pumpkin (CucurbitaPepo L.) oil cake protein isolate, Response surface methodology.
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