In vitro study on antioxidant activities of peanut protein hydrolysate

Peanut protein was hydrolysed with a commercial protease, Alcalase 2.4L, and the resulting hydrolysate was investigated for its antioxidant activities, including the ability to inhibit the autoxidation of linoleic acid, the scavenging effect on the 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH) free radical, the reducing power and the inhibition of liver lipid oxidation. As compared with the peanut protein, peanut protein hydrolysate showed strong inhibition of the autoxidation of linoleic acid, to scavenge DPPH free radical and showed strong reducing power. Moreover, peanut protein hydrolysate also displayed noticeable inhibition of liver lipid autoxidation and lipid oxidation induced by H₂O₂ or Fe²⁺ in vitro. All these effects of the sample were concentration‐dependent. These results suggest that peanut protein hydrolysate could be a suitable natural antioxidant and may be a health food for humans. Copyright © 2006 Society of Chemical Industry     

Physicochemical and antioxidant properties of Maillard reaction products formed by heating whey protein isolate and reducing sugars

This study was conducted to investigate the physicochemical and antioxidant properties of Maillard reaction products (MRP) prepared by heating whey protein isolate (WPI) and reducing sugars (glucose and galactose) to 95 °C for different lengths of time (0–6 h). The results revealed that the colour, intermediate products, browning intensity and the antioxidant activities of the MRP increased as the reaction time increased (P < 0.05), whereas the pH value and free amino group content decreased (P < 0.05). Sodium dodecyl sulphate–polyacrylamide gel electrophoresis indicated that the covalently linked conjugates of WPI and sugars were formed. The results indicate that the Maillard reaction could improve the antioxidant capacity of WPI.     

Impact of ultrafiltration and nanofiltration of an industrial fish protein hydrolysate on its bioactive properties

BACKGROUND: Numerous studies have demonstrated that in vitro controlled enzymatic hydrolysis of fish and shellfish proteins leads to bioactive peptides. Ultrafiltration (UF) and/or nanofiltration (NF) can be used to refine hydrolysates and also to fractionate them in order to obtain a peptide population enriched in selected sizes. This study was designed to highlight the impact of controlled UF and NF on the stability of biological activities of an industrial fish protein hydrolysate (FPH) and to understand whether fractionation could improve its content in bioactive peptides. RESULTS: The starting fish protein hydrolysate exhibited a balanced amino acid composition, a reproducible molecular weight (MW) profile, and a low sodium chloride content, allowing the study of its biological activity. Successive fractionation on UF and NF membranes allowed concentration of peptides of selected sizes, without, however, carrying out sharp separations, some MW classes being found in several fractions. Peptides containing Pro, Hyp, Asp and Glu were concentrated in the UF and NF retentates compared to the unfractionated hydrolysate and UF permeate, respectively. Gastrin/cholecystokinin‐like peptides were present in the starting FPH, UF and NF fractions, but fractionation did not increase their concentration. In contrast, quantification of calcitonin gene‐related peptide (CGRP)‐like peptides demonstrated an increase in CGRP‐like activities in the UF permeate, relative to the starting FPH. The starting hydrolysate also showed a potent antioxidant and radical scavenging activity, and a moderate angiotensin‐converting enzyme (ACE)‐1 inhibitory activity, which were not increased by UF and NF fractionation. CONCLUSION: Fractionation of an FPH using membrane separation, with a molecular weight cut‐off adapted to the peptide composition, may provide an effective means to concentrate CGRP‐like peptides and peptides enriched in selected amino acids. The peptide size distribution observed after UF and NF fractionation demonstrates that it is misleading to characterize the fractions obtained by membrane filtration according to the MW cut‐off of the membrane only, as is currently done in the literature. Copyright © 2010 Society of Chemical Industry     

Influence of degree of hydrolysis on functional properties,antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate

Functional properties, antioxidant and Angiotensin-converting enzyme (ACE) inhibitory activities of peanut protein isolate (PPI) and peanut protein hydrolysate (PPH) prepared using Alcalase, at different (10%, 20%, 30% and 40%) degrees of hydrolysis, (DH) were investigated. Hydrolysis (at DH > 10%) significantly (p < 0.05) improved the solubility (>80%) of PPI, especially in the pH range of 4–6. However, PPI showed better emulsifying and foaming properties than PPH (p < 0.05). As DH increased, ferrous ion chelating activity, 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical-scavenging activity and ACE inhibitory activity of PPH increased, while reducing power decreased (p < 0.05). Bleaching of beta-carotene by linoleic acid was suppressed better by PPI and PPH at 10% DH than of PPH at higher DH. Thus, the results reveal that DH affects functional properties, antioxidant and ACE inhibitory activities of peanut protein.     

红衣组分对花生分离蛋白及其酶解产物理化和抗氧化性质的影响

以花生为原料,研究了花生红衣组分对花生分离蛋白及其酶解产物理化和抗氧化性质的影响。研究结果表明:含红衣的分离蛋白酶解速度低于不含红衣的;相同水解度条件下,含红衣的表面疏水性小于脱红衣的;GPC分布中,含红衣的峰值大于脱红衣的;红衣组分能够提高花生分离蛋白及其酶解产物的溶解性、乳化稳定性、乳化活性;在相同水解度条件下,含红衣的水解产物多酚含量显著高于脱红衣的,多酚含量的差异与花生分离蛋白及其水解产物的抗氧化性具有正相关性。     

Functional and antioxidative properties of protein hydrolysates from Cape hake by‐products prepared by three different methodologies

BACKGROUND: The production of fish protein hydrolysates (FPH) is a convenient technology for upgrading fish by‐products. The aim of this work was to study three different methods of FPH preparation from Cape hake by‐products to improve yield and quality. Functional and antioxidative properties of all FPHs were determined. RESULTS: The protein content of hake FPH was in the range 807–860 g kg^?1 and the degree of hydrolysis was between 19% and 22%. The maximum yield (71.9%) was achieved by methodology B but the hydrolysate was darker. The peptide profile of all FPHs was very similar. FPH prepared by methodology C had significantly higher emulsifying activity index and hydrolysate prepared by methodology B had the highest foaming capacity. The solubility of FPH was in the range 71–76% and increased the water‐holding capacity of minced fish by about 9%. The fractionation of FPH obtained by methodologies A and B allowed concentrating peptides with higher radical scavenging activity and reducing power. CONCLUSION: The properties of the FPH prepared indicated that they can be used in food systems as natural additives, particularly to improve their water‐holding capacity. © 2012 Society of Chemical Industry     

超高压协同酶法条件下不同分子量大豆分离蛋白水解肽乳化性及抗氧化性研究

目的研究不同分子量分布对大豆分离蛋白水解肽乳化性及抗氧化性的影响。方法采用超滤技术将超高压协同酶解制备的大豆分离蛋白水解物分离得到5个分子量肽段,即分子量（Molecular weight, Mw）<3500 u、3500 u< Mw <7000 u、7000 u< Mw <10000 u、10000 u< Mw <20000 u和Mw >20000 u。通过测定乳化活性、乳化稳定性、电势、粒径、还原力、以及对 2,2-联苯基-1-苦基肼基(2,2-diphenyl-1-picrylhydrazyl, DPPH)和 2,2''-联氮-双(3-乙基苯并噻唑-6-磺酸)（2, 2-azinobis (3-ethylbenzothiazoline-6-sulfonic acid), ABTS）自由基清除率,分析不同分子量水解肽的乳化性及抗氧化性变化。结果7000 u< Mw <10000 u的水解肽具有较高的乳化活性、电势和较小的粒径,而10000 u< Mw <20000 u的水解肽则表现出较优的乳化稳定性,但与7000 u< Mw <10000 u的组分差异不显著(P＞0.05);水解肽的抗氧化性随肽段分子量的减小呈逐渐增大趋势,且不同分子量肽段与还原力和DPPH自由基清除能力均呈极显著负相关性（P＜0.01）,与ABTS自由基清除能力呈显著负相关性(P＜0.05)。结论 超高压协同酶法制备的大豆分离蛋白水解肽,乳化性和抗氧化性与其分子量分布有密切关联,这为相关功能性产品的开发提供了较为切实的理论依据。     

Identification of angiotensin converting enzyme inhibitory and antioxidant peptides in a whey protein concentrate hydrolysate produced at semi‐pilot scale

Antioxidant and angiotensin converting enzyme (ACE) inhibitory peptides were identified in a 5 kDa ultrafiltration permeate of a whey protein hydrolysate generated at semi‐pilot scale. Further laboratory scale ultrafiltration of this 5 kDa permeate resulted in a 0.65 kDa permeate with antioxidant, (1.11 ± 0.074 μmol TE per mg dry weight, oxygen radical absorbance capacity, ORAC) and ACE inhibitory (ACE IC₅₀ 0.215 ± 0.043 mg mL^?1) activities. Semi‐preparative (SP) reverse phase high‐performance liquid chromatography (RP‐HPLC) of the 0.65 kDa permeate resulted in a fraction (SP_F3) with a 4.4‐fold increase in ORAC activity (4.83 ± 0.45 μmol TE mg dry weight) and a 1.3‐fold increase in ACE inhibitory activity (84.35 ± 1.36% inhibition when assayed at 0.28 mg mL^?1). Peptides within SP_F3 were identified using UPLC‐ESI‐MS/MS. Met‐Pro‐Ile had the highest ORAC activity (205.75 ± 12.08 μmol TE per mmol peptide) while Met‐Ala‐Ala and Val‐Ala‐Gly‐Thr had the highest ACE inhibitory activities (IC₅₀:515.50 ± 1.11 and 610.30 ± 2.41 μm , respectively).     

The effects of salt concentration and pH upon water-binding, water-holding and protein extractability of turkey meat

The effects of salt concentration and pH upon protein extractability and water-binding by homogenates of turkey breast, thigh and drumstick meat, and also the effect of salt concentration and centrifugal force upon water-binding of raw meat and water-holding of cooked meat from breast and thigh were studied. Concentrations of sodium chloride above 0.3 M caused swelling of meat homogenates. With the pH value adjusted to 6.0 and with sodium chloride concentrations greater than 0.6 M, breast meat was able to swell more than leg meat. Water-binding increased with increasing pH value. Breast meat homogenates had more extractable protein than leg meat homogenates and protein extraction was increased by increasing both salt concentration and pH. Cooked breast meat retained more water than leg meat with or without salt. At low concentrations of salt, cooked breast meat retained more water than raw meats, but this was reversed at higher salt concentrations.