In today’s study whey protein concentrate (WPC-80) and β-lactoglobulin were hydrolyzed

In today’s study whey protein concentrate (WPC-80) and β-lactoglobulin were hydrolyzed having a noncommercial serine protease isolated from SEA0400 Asian pumpkin (alkaline protease indicated similar activity (Matsui et al. of bioactive peptides the antihypertensive peptides are the best known. ACE SEA0400 inhibitory peptides have been discovered in various food sources such as milk gelatine maize and soybean (Meisel 1997; Oshima et al. 1979; Miyoshi et al. 1991 Okamoto et al. 1995). Antihypertensive peptides have been found in processed dairy products. ACE inhibitors derived from milk proteins represent different fragments of casein (casokinins) or whey proteins (lactokinins) (Nakamura et al. 1995; Korhonen and Pihlanto-Lepp?l? 2006). Two potent ACE-inhibitory peptides from β-casein f84-f86 which corresponds to Val-Pro-Pro and f74-f76 which corresponds to Ile-Pro-Pro and one from k-casein f108-f110 which corresponds to Ile-Pro-Pro were purified from the Japanese soft drink “Calpis” made from bovine skim milk fermented with and (Nakamura et al. 1995). The results of Pihlanto’s study demonstrate the living of several biologically active whey-derived peptides and hydrolysates (Pihlanto 2000). Whey proteins are significantly resistant to hydrolysis and the use of enzymes significantly increases the cost of their production. One of the encouraging alternatives is the use of flower serine protease isolated from exhibiting attractive proteolytic properties towards casein protein from corn gluten meal (CGM) or ovoalbumin (Illanes et al. 1985; Curotto et al. 1989; Pokora et al. 2014). The protease exhibits an extremely broad and high pH optimum using a optimum at 10.7 and can cleave four bonds within an endogenous serine proteinase inhibitor. The ideal temperature is normally 35?°C and ideal pH is 8.6 (Dryjańskiing et al. 1990). Acquiring this into consideration we utilized serine protease from to hydrolyze whey protein to create peptides with antidiabetic and antyhipertensive actions. The aim of this study is to investigate peptides generated from whey proteins hydrolyzed from the CD117 non-commercial proteolytic enzyme from Asian pumpkin as the natural sources of DPP-IV α-glucosidase and ACE inhibitors that can be used as functional food elements for the complex management of type 2 diabetes and hypertension. Materials and Methods Isolation of the Enzyme Serine protease was isolated from Asian pumpkin according to the method of Dryjański et al. (1990). After separating the peel from the seeds the pulp was homogenized and centrifuged at 5 0 G0660) hydrolyzed the substrate-were also assessed for his or her inhibitory activity against α-glucosidase SEA0400 (Fig.?4a-d). Among fifteen peptide fractions derived from the WPC-80 hydrolysate with the molecular mass below 3?kDa thirteen exhibited α-glucosidase inhibitory activity (Fig.?4c). Within this group six fractions showed the greatest potency with the IC50 ideals below 2.0?mg/mL. However when we compared the results with those of β-lactoglobulin peptide fractions of the same molecular mass range only four fractions displayed the inhibiting activity. The relatively low inhibitory activity was amazing SEA0400 because β-lactoglobulin is the major protein portion in whey. In addition in the paper of Lacroix and Li-Chan (2013) α-lactalbumin lactoferrin and serum albumin hydrolysates acquired by peptic digestion were able to inhibit the activity of α-glucosidase. Fig.?4 α-Glucosidase inhibitory activity of β-lactoglobulin (a b) and WPC derived peptide fractions (c d). β-lactoglobulin fractions of molecular mass <3?kDa (a) 3 (b). WPC fractions of molecular ... The only study on α-glucosidase inhibitory activity of whey protein hydrolysates was carried out by Lacroix and Li-Chan (2013). The inhibitory activity towards α-glucosidase was observed only in case of WPI (IC50?=?4.5?mg/mL) and β-lactoglobulin (IC50?=?3.5?mg/mL). The different levels of this activity in their study might have resulted from the use of rat intestinal α-glucosidase in the assay (Lacroix and Li-Chan 2013 Some synthetic inhibitors show different ability to inhibit the activity of α-glucosidase depending on the enzyme origin. They strongly affect the activity of mammalian α-glucosidase but have little inhibitory effect on baker’s yeast.