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1.
The functional characteristics which include protein solubility at different pH, emulsifying and foaming properties, degree of hydrolysis, molecular weight distribution, antioxidant and ACE inhibitory activity of sesame protein hydrolysates prepared with pepsin, papain and alcalase enzymes were evaluated. The rate of degree of hydrolysis was found to reach maximum (25–30%) within the first time fragment i.e 10 min but 80% of hydrolysis was obtained in 120 min with alcalase. SDS-PAGE of hydrolysates with papain, pepsin and alcalase evinced bands of low molecular weight protein of 14.3 kDa and even lower for alcalase treatment of 120 min. Hydrolysates so formed were of improved functional properties as evident from emulsifying and foaming property. Hydrolysis with different proteases enhanced the protein solubility significantly at pH 7.0. Antioxidative assay revealed radical scavenging activity of the hydrolysates with papain hydrolysates showing maximum antioxidative efficacy. The ultra-filtered peptide fractions which showed comparable ACE inhibitory activity were sequenced by MALDI-TOF and matched to that of previously identified ACE inhibitory peptides. The results corroborate the ACE inhibitory effect of the peptides. Hence, these highly bioactive protein hydrolysates produced from waste sesame meals can be successfully employed in various functional food formulations. 相似文献
2.
Raheleh Ghanbari Mohammad Zarei Afshin Ebrahimpour Azizah Abdul-Hamid Amin Ismail Nazamid Saari 《International journal of molecular sciences》2015,16(12):28870-28885
In recent years, food protein-derived hydrolysates have received considerable attention because of their numerous health benefits. Amongst the hydrolysates, those with anti-hypertensive and anti-oxidative activities are receiving special attention as both activities can play significant roles in preventing cardiovascular diseases. The present study investigated the angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidative activities of Actinopyga lecanora (A. lecanora) hydrolysates, which had been prepared by alcalase, papain, bromelain, flavourzyme, pepsin, and trypsin under their optimum conditions. The alcalase hydrolysate showed the highest ACE inhibitory activity (69.8%) after 8 h of hydrolysis while the highest anti-oxidative activities measured by 2,2-diphenyl 1-1-picrylhydrazyl radical scavenging (DPPH) (56.00%) and ferrous ion-chelating (FIC) (59.00%) methods were exhibited after 24 h and 8 h of hydrolysis, respectively. The ACE-inhibitory and anti-oxidative activities displayed dose-dependent trends, and increased with increasing protein hydrolysate concentrations. Moreover, strong positive correlations between angiotensin-I converting enzyme (ACE) inhibitory and anti-oxidative activities were also observed. This study indicates that A. lecanora hydrolysate can be exploited as a source of functional food owing to its anti-oxidant as well as anti-hypertension functions. 相似文献
3.
Alvaro Montoya-Rodríguez Jorge Milán-Carrillo Cuauhtémoc Reyes-Moreno Elvira González de Mejía 《International journal of molecular sciences》2015,16(4):8536-8554
The objectives of this study were to characterize peptides found in unprocessed amaranth hydrolysates (UAH) and extruded amaranth hydrolysates (EAH) and to determine the effect of the hydrolysis time on the profile of peptides produced. Amaranth grain was extruded in a single screw extruder at 125 °C of extrusion temperature and 130 rpm of screw speed. Unprocessed and extruded amaranth flour were hydrolyzed with pepsin/pancreatin enzymes following a kinetic at 10, 25, 60, 90, 120 and 180 min for each enzyme. After 180 min of pepsin hydrolysis, aliquots were taken at each time during pancreatin hydrolysis to characterize the hydrolysates by MALDI-TOF/MS-MS. Molecular masses (MM) (527, 567, 802, 984, 1295, 1545, 2034 and 2064 Da) of peptides appeared consistently during hydrolysis, showing high intensity at 10 min (2064 Da), 120 min (802 Da) and 180 min (567 Da) in UAH. EAH showed high intensity at 10 min (2034 Da) and 120 min (984, 1295 and 1545 Da). Extrusion produced more peptides with MM lower than 1000 Da immediately after 10 min of hydrolysis. Hydrolysis time impacted on the peptide profile, as longer the time lower the MM in both amaranth hydrolysates. Sequences obtained were analyzed for their biological activity at BIOPEP, showing important inhibitory activities related to chronic diseases. These peptides could be used as a food ingredient/supplement in a healthy diet to prevent the risk to develop chronic diseases. 相似文献
4.
Process parameters on enzymatic hydrolysis and molecular weight (MW) distribution of whey protein hydrolysates were investigated. Whey protein hydrolysates were first gained by the alkaline protease alcalase for 7 h at temperature (50 °C), pH (8.0) and E/S (3%). The diversification of the hydrolysis degree and dissociative amino acid content was investigated during the whey hydrolysis. The dissociative amino acid content was 56.09 μmol/mL with the hydrolysis degree of 20.04%. The results of Sephadex G25 washing and high performance liquid chromatography–electrospray ionization–mass spectrometry (HPLC–ESI–MS) indicated the molecular weight distribution of whey protein hydrolysates ranged from 300 to 1400 Da, and most of whey peptide was under 1000 Da. 相似文献
5.
M Zarei A Ebrahimpour A Abdul-Hamid F Anwar N Saari 《International journal of molecular sciences》2012,13(7):8097-8111
The aim of this study was to produce a valuable protein hydrolysate from palm kernel cake (PKC) for the development of natural antioxidants. Extracted PKC protein was hydrolyzed using different proteases (alcalase, chymotrypsin, papain, pepsin, trypsin, flavourzyme, and bromelain). Subsequently, antioxidant activity and degree of hydrolysis (DH) of each hydrolysate were evaluated using DPPH• radical scavenging activity and O-phthaldialdehyde spectrophotometric assay, respectively. The results revealed a strong correlation between DH and radical scavenging activity of the hydrolysates, where among these, protein hydrolysates produced by papain after 38 h hydrolysis exhibited the highest DH (91 ± 0.1%) and DPPH• radical scavenging activity (73.5 ± 0.25%) compared to the other hydrolysates. In addition, fractionation of the most effective (potent) hydrolysate by reverse phase high performance liquid chromatography indicated a direct association between hydrophobicity and radical scavenging activity of the hydrolysates. Isoelectric focusing tests also revealed that protein hydrolysates with basic and neutral isoelectric point (pI) have the highest radical scavenging activity, although few fractions in the acidic range also exhibited good antioxidant potential. 相似文献
6.
Abraham T. Girgih Chibuike C. Udenigwe Rotimi E. Aluko 《Journal of the American Oil Chemists' Society》2011,88(3):381-389
Simulated gastrointestinal hydrolysis of hemp seed proteins using pepsin and pancreatin followed by membrane ultrafiltration
fractionation yielded fractions with peptide sizes of <1, 1–3, 3–5, and 5–10 kDa. Analysis of in vitro antioxidant properties
showed that the hemp seed protein hydrolysate (HPH) exhibited a significantly weaker (p < 0.05) scavenging of 2,2-diphenyl-1-picrylhydrazyl (DPPH) radicals when compared to the fractionated peptides. Metal chelation
activity of the HPH was significantly greater (p < 0.05) than the activities of fractionated peptides. Fractionation of the HPH led to significant (p < 0.05) improvements in ferric reducing power, DPPH, and hydroxyl radical scavenging radical activities but decreased metal
chelation capacity. Peptide fractions with longer chain lengths (3–5 and 5–10 kDa) had better metal chelation and ferric reducing
power than the <1, and 1–3 kDa fractions. HPH and all the peptide fractions significantly inhibited (p < 0.05) linoleic acid oxidation when compared to the control. Glutathione (GSH) had significantly greater (p < 0.05) ferric reducing power, and scavenging of hydroxyl and DPPH radicals when compared to HPH and fractionated peptides.
In contrast, HPH and peptide fractions >3 kDa had significantly higher (p < 0.05) metal chelation activity than GSH. The results show the potential use of HPH and peptide fractions of defined size
for the treatment of oxidative stress-related diseases. 相似文献
7.
Xubo Fang Ningning Xie Xiaoe Chen Hui Yu Jing Chen 《Food and Bioproducts Processing》2012,90(4):676-682
The squid muscle protein, extracted from by-products of flying squid (Ommastrephes bartrami) was hydrolyzed by five proteases (pepsin, trypsin, papain, alcalase and flavourzyme). DPPH radical scavenging power was used to evaluate antioxidative activity of hydrolysates. The hydrolysate obtained by papain exhibited the most excellent potential of antioxidative activity. Furthermore, response surface methodology (RSM) was employed to optimize hydrolysis conditions, including enzyme to substrate (E/S) ratio, reaction temperature, and hydrolysis time. The optimum conditions obtained were as follows: E/S ratio of 1.74%, temperature of 51 °C and time of 46 min, under which, DPPH radical scavenging activity of 74.25% was obtained. Moreover, it was found that the optimum hydrolysate of 8 mg/mL displayed relatively stronger inhibitory effect on lipid peroxidation compared with α-Tocopherol of 0.1 mg/mL. 相似文献
8.
Amino Acid Profiles of 44 Soybean Lines and ACE‐I Inhibitory Activities of Peptide Fractions from Selected Lines
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Srinivas Rayaprolu Navam Hettiarachchy Ronny Horax Eswaranandam Satchithanandam Pengyin Chen Andy Mauromoustakos 《Journal of the American Oil Chemists' Society》2015,92(7):1023-1033
Soybeans are cultivated in the United States chiefly for cooking oil, while the residue after oil extraction (soybean meal) is mostly used in animal feed formulations. High protein content in the defatted soybean meals led to the extraction of pure protein and its application in food products. We selected 44 soybean lines to determine their moisture and protein contents, and their amino acid composition was investigated. Soybean lines with high protein content, one high yielding (R95‐1705), and two high oleic acid (N98‐4445A, S03‐543CR), were selected for protein isolate preparation, hydrolysis using alcalase and gastro‐intestinal (GI) resistance. Furthermore, the GI resistant hydrolysates were fractionated and tested for angiotensin‐I‐converting enzyme (ACE‐I) inhibition activity. The amino acid analysis showed high methionine in the high protein and fatty acid lines (R05‐4494 and R05‐5491), and high cysteine content in one of the high oleic acid soybean line CRR05‐188 in comparison to the check lines (UA‐4805 and 5601‐T). The protein isolate with the highest purity (90–93 %) was derived from the selected lines N98‐4445A and S03‐543CR, and hydrolyzed using alcalase enzyme. The protein hydrolysates (500 µg/mL) showed inhibition of the ACE‐I by 49 %. The results from this study will promote the use of high oleic acid soybeans as a source of protein and peptides with functional activities. 相似文献
9.
Ljiljana Popović Draginja Peričin Žužana Vaštag Senka Popović Vera Krimer Aleksandra Torbica 《Journal of the American Oil Chemists' Society》2013,90(8):1157-1165
Cucurbitin extracted from pumpkin (Cucurbita pepo) oil cake was enzymatically hydrolysed with three different enzymes viz. alcalase, flavourzyme and pepsin. Antioxidative and functional properties of cucurbitin hydrolysates with different degrees of hydrolysis (DH) were investigated. The antioxidant activity of the hydrolysates was strongly dependent on the enzyme used. The hydrolysates obtained by alcalase and pepsin showed antioxidative potential whereas flavourzyme hydrolysates did not demonstrate these activities. Reducing power and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) (ABTS) scavenging activity of cucurbitin hydrolysate were positively related to DH. The highest antioxidant activity was found in the hydrolysate obtained by alcalase at DH 25.6 % [reducing power of 0.25 ± 0.01 A700 nm and ABTS scavenging activity of 3.34 ± 0.02 mmol/L Trolox equivalent antioxidant coefficients (TEAC)]. Hydrolysis by all enzymes increased the protein solubility within the studied pH range. The best emulsion activity and stability index (EAI = 143.28 ± 3.05 m2/g and ESI = 87.5 ± 1.96 min) have hydrolysates produced by flavourzyme (DH 9.2 %) whereas alcalase produced hydrolysates with the best foaming capacity (FC = 242 ± 3.21). The results demonstrate that hydrolysates produced in the present study have good functional properties as well as antioxidant activity indicating their possible use in different food systems. 相似文献
10.
Liyuan Liu Yanping Wang Chen Peng Jinju Wang 《International journal of molecular sciences》2013,14(2):3124-3139
The enzymatic condition for producing the anti-obesity hydrolysates from fish water-soluble protein was optimized with the aid of response surface methodology, which also derived a statistical model for experimental validation. Compared with neutral protease, papain and protamex, the porcine pancreas lipase inhibitory rate of hydrolysates from fish water-soluble protein was higher with alkaline protease. Results showed that the model terms were significant, the terms of lack of fit were not significant, and the optimal conditions for the hydrolysis by alkaline protease were initial pH 11, temperature 39 °C, enzyme dosage 122 U/mL and 10 h of hydrolysis time. Under these conditions, the porcine pancreas lipase and the α-amylase inhibitory rate could reach 53.04% ± 1.32% and 20.03 ± 0.89%, while predicted value were 54.63% ± 1.75%, 21.22% ± 0.70%, respectively. In addition, Lineweaver-Burk plots showed noncompetitive inhibition. The Ki value calculated was 84.13 mg/mL. These results demonstrated that fish water-soluble protein could be used for obtaining anti-obesity hydrolysates. 相似文献
11.
Analysis of products, mechanisms of reaction, and some functional properties of soy protein hydrolysates 总被引:11,自引:0,他引:11
Sara E. Molina Ortiz Mara Cristina An 《Journal of the American Oil Chemists' Society》2000,77(12):1293-1301
Soybean protein isolates were hydrolyzed with papain, bromelain, cucurbita, hieronymin, and pomiferin. The highest hydrolysis
rate for cucurbita and the lowest for papain was detected at 720 min. Gel filtration, reversed-phase liquid chromatography,
and electrophoresis showed that the action of each protease was different. Pomiferin acted on the native structure of β-conglycinin
and glycinin, generating a large number of small hydrolysis products with hydrophilic and hydrophobic characteristics. The
hydrolysates obtained with cucurbita showed residual structures that were almost intact and very similar to the substrate
and contained a low number of small peptides. The hydrolyzates obtained with papain, bromelain, and hieronymin had hydrolysis
products with structures similar to the partially hydrolyzed native isolate. The molecular masses of these products were similar
to or lower than the controls. Polypeptides of low molecular mass were also detected. The prevalence of one-by-one and zipper
mechanisms was suggested for cucurbita and pomiferin, respectively. For the other proteases both mechanisms were likely to
coexist. The solubility of hydrolysates and their ability to form and stabilize foams correlated well with the structural
properties and with the suggested mechanisms of hydrolysis. The best properties were presented by the hydrolysates prepared
with cucurbita. Foaming ability for pomiferin hydrolysates was as high as that for unhydrolyzed soy isolate, but the foams
were extremely unstable. 相似文献
12.
In vitro antioxidant activity of enzymatic hydrolysates prepared from abalone (Haliotis discus hannai Ino) viscera 总被引:1,自引:0,他引:1
Da-Yong Zhou Bei-Wei Zhu Lu Qiao Hai-Tao Wu Dong-Mei Li Jing-Feng Yang Yoshiyuki Murata 《Food and Bioproducts Processing》2012,90(2):148-154
Pacific abalone (Haliotis discus hannai Ino) viscera, which are normally discarded as byproducts, were hydrolyzed with five commercially available proteases, including alkali protease, papain, neutral protease, pepsin, and trypsin. The hydrolysates obtained were fractionated using ultrafiltration membrane bioreactor system. The resulting hydrolysate fractions were investigated for their antioxidant activities, including the scavenging effect on 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, the scavenging effect on hydroxyl radical, and the reducing power. Results showed that the hydrolysate fractions were effective antioxidants, and the antioxidant activity of the hydrolysates was related to the enzyme type employed. As byproducts, abalone viscera can be used as a potential source of antioxidant peptides. 相似文献
13.
Abraham T. Girgih Chibuike C. Udenigwe Huan Li Abayomi P. Adebiyi Rotimi E. Aluko 《Journal of the American Oil Chemists' Society》2011,88(11):1767-1774
The aim of this study was to determine the antihypertensive effects of enzymatic hemp seed protein hydrolysate (HPH) and its
peptide fractions. Hemp seed protein isolate was digested by the sequential action of pepsin and pancreatin to mimic gastrointestinal
digestion in human beings. The resultant HPH was separated by membrane ultrafiltration into peptide fractions with different
sizes (<1 and 1–3 kDa). The HPH led to significantly higher (P < 0.05) in vitro inhibition of the activities of angiotensin I-converting enzyme (ACE) and renin, the two main enzymes involved
in abnormal blood pressure elevation (hypertension). Kinetic studies showed that HPH and peptide fractions inhibited renin
and ACE activities in a mixed-type pattern, indicating binding to areas other than the active site. Oral administration of
HPH (200 mg/kg body weight) to spontaneously hypertensive rats led to significant reductions (P < 0.05) in systolic blood pressure (SBP) that reached a maximum of −30 mmHg after 8 h. In contrast, the hypotensive effects
of peptide fractions (<1 and 1–3 kDa) had a maximum value of about −15 mmHg after 6–8 h post oral administration. The results
suggest a synergistic antihypertensive effect of the peptides present within HPH; this effect was reduced significantly (P < 0.05) upon separation into peptide fractions. 相似文献
14.
15.
Optimization of the Aqueous Enzymatic Extraction of Rapeseed Oil and Protein Hydrolysates 总被引:3,自引:0,他引:3
Shao Bing Zhang Zhang Wang Shi Ying Xu 《Journal of the American Oil Chemists' Society》2007,84(1):97-105
An aqueous enzymatic extraction method was developed to obtain free oil and protein hydrolysates from dehulled rapeseeds.
The rapeseed slurry was treated by the chosen combination of pectinase, cellulase, and β-glucanase (4:1:1, v/v/v) at concentration
of 2.5% (v/w) for 4 h. This was followed by sequential treatments consisting of alkaline extraction and an alkaline protease
(Alcalase 2.4L) hydrolysis to both produce a protein hydrolysate product and demulsify the oil. Response surface methodology
(RSM) was used to study and optimize the effects of the pH of the alkaline extraction (9.0, 10.0 and 11.0), the concentration
of the Alcalase 2.4L (0.5, 1.0 and 1.5%, v/w), and the duration of the hydrolysis (60, 120, and 180 min). Increasing the concentration
of Alcalase 2.4L and the duration of the hydrolysis time significantly increased the yields of free oil and protein hydrolysates
and the degree of protein hydrolysis (DH), while the alkaline extraction pH had a significant effect only on the yield of
the protein hydrolysates. Following an alkaline extraction at pH 10 for 30 min, we defined a practical optimum protocol consisting
of a concentration of 1.25–1.5% Alcalase 2.4L and a hydrolysis time between 150 and 180 min. Under these conditions, the yields
of free oil and protein hydrolysates were 73–76% and 80–83%, respectively. The hydrolysates consisted of approximately 96%
of peptides with a MW less than 1500, of which about 81% had a MW less than 600 Da. 相似文献
16.
Hydrophobicity, solubility, and emulsifying properties of soy protein peptides prepared by papain modification and ultrafiltration 总被引:15,自引:5,他引:10
W. U. Wu N. S. Hettiarachchy M. Qi 《Journal of the American Oil Chemists' Society》1998,75(7):845-850
Peptide size control is important for obtaining desirable functional properties so that these peptides can be better utilized.
Proteolytic enzymatic modification of soy protein isolates (SPI), followed by ultrafiltration, is an effective way to fractionate
these proteins into peptides with controlled molecular size. SPI was predenatured by mild alkali at pH 10 and heated at 50°C
for 1 h prior to partial hydrolysis by papain at pH 7.0 and 38°C for 10, 30, and 60 min (PMSPI10, PMSPI30, and PMSPI60). The
hydrolysate PMSPI60 was further fractionated by ultrafiltration with a stirred cell and disc membranes (100-, 50-, and 20-kDa
molecular weight cut-off) into one retentate (R100) and three permeates (P100, P50, and P20). Molecular weight distribution,
surface hydrophobicity (S
0), protein solubility (PS), emulsifying activity index (EAI), and emulsion stability index (ESI) of the control SPI (without
added papain), hydrolysates, and ultrafiltrates were investigated. Significant increases (P<0.001) in S
0, PS, EAI, and ESI were observed in the hydrolysates. Peptides in the permeates had higher PS and EAI but lower S
0 than the peptides in the retentate and hydrolysate. Soy protein peptides that were prepared from SPI by papain modification
and ultrafiltration had lower molecular weight, higher solubility, and higher emulsifying properties. They could find use
in products that require these properties, especially in the cosmetic and health food industries. 相似文献
17.
18.
Y Xie X Liang M Wei W Zhao B He Q Lu Q Huo C Ma 《International journal of molecular sciences》2012,13(6):7483-7495
The process parameters of enzymatic hydrolysis and molecular weight distribution of glutamine (Gln) peptides from soybean meal were investigated. The Protamex® hydrolysis pH of 6.10, temperature of 56.78 °C, enzyme to substrate ratio (E/S) of 1.90 and hydrolysis time of 10.72 h were found to be the optimal conditions by response surface methodology (RSM) for a maximal degree of hydrolysis (DH) value of 16.63% and Gln peptides content at 5.95 mmol/L. The soybean meal was hydrolyzed by a combination of Protamex® and trypsinase so that DH and Gln peptides would reach 22.02% and 6.05 mmol/mL, respectively. The results of size exclusion chromatography indicated that the relative proportion of the molecular weight <1000 Da fraction increased with DH values from 6.76%, 11.13%, 17.89% to 22.02%, most notably the 132–500 Da fractions of hydrolysates were 42.14%, 46.57%, 58.44% and 69.65%. High DH values did not lead to high Gln peptides content of the hydrolysate but to the low molecular weight Gln peptides. 相似文献
19.
Ma?gorzata Darewicz Justyna Borawska Gerd E. Vegarud Piotr Minkiewicz Anna Iwaniak 《International journal of molecular sciences》2014,15(8):14077-14101
The objectives of the present study were two-fold: first, to detect whether salmon protein fractions possess angiotensin I-converting enzyme (ACE) inhibitory properties and whether salmon proteins can release ACE inhibitory peptides during a sequential in vitro hydrolysis (with commercial porcine enzymes) and ex vivo digestion (with human gastrointestinal enzymes). Secondly, to evaluate the ACE inhibitory activity of generated hydrolysates. A two-step ex vivo and in vitro model digestion was performed to simulate the human digestion process. Salmon proteins were degraded more efficiently by porcine enzymes than by human gastrointestinal juices and sarcoplasmic proteins were digested/hydrolyzed more easily than myofibrillar proteins. The ex vivo digested myofibrillar and sarcoplasmic duodenal samples showed IC50 values (concentration required to decrease the ACE activity by 50%) of 1.06 and 2.16 mg/mL, respectively. The in vitro hydrolyzed myofibrillar and sarcoplasmic samples showed IC50 values of 0.91 and 1.04 mg/mL, respectively. Based on the results of in silico studies, it was possible to identify 9 peptides of the ex vivo hydrolysates and 7 peptides of the in vitro hydrolysates of salmon proteins of 11 selected peptides. In both types of salmon hydrolysates, ACE-inhibitory peptides IW, IY, TVY and VW were identified. In the in vitro salmon protein hydrolysates an ACE-inhibitory peptides VPW and VY were also detected, while ACE-inhibitory peptides ALPHA, IVY and IWHHT were identified in the hydrolysates generated with ex vivo digestion. In our studies, we documented ACE inhibitory in vitro effects of salmon protein hydrolysates obtained by human and as well as porcine gastrointestinal enzymes. 相似文献
20.
Biologically Active Digests from Pumpkin Oil Cake Protein: Effect of Cross-linking by Transglutaminase
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Ljiljana Popović Žužana Stolić Jelena Čakarević Aleksandra Torbica Jelena Tomić Mirjana Šijački 《Journal of the American Oil Chemists' Society》2017,94(10):1245-1251
The objective of this study was to show that biologically active hydrolysates can be obtained by simulated human gastrointestinal digestion (HGD) of transglutaminase cross-linked pumpkin oil cake protein (Tg-C) which was previously reported as a potential functional food additive. A two-stage in vitro digestion model system (by pepsin and α chymotrypsin and trypsin, simultaneously) was used to simulate the process of HGD on native and Tg-C major storage pumpkin oil seed/cake protein, cucurbitin (C). The biologically active potential of the digests was evaluated, measuring the angiotensin-converting-I enzyme (ACE) inhibitory and anti-oxidant capacity. The ACE inhibitory activity was determined in both final digests, with IC50 = 0.30 ± 0.04 mg/ml for C and IC50 = 0.28 ± 0.01 for Tg-C. The anti-oxidant potency of the examined proteins was enhanced by the digestion process. The 2,2-diphenyl-1-picrylhydrazyl and 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid) radical cation activities and reducing power testing showed that all the hydrolysates act as a radical quencher and reducing agents. Overall, the results showed that the cross-linking by Tg did not influence the digestion process, as well as having no effect on the biological activity of the hydrolysates. These also indicate that Tg-C, if used as functional food additive, after food consumption can be digested and become a source of peptides exerting positive effects on human health. 相似文献