Effect of power ultrasound pretreatment on peptidic profiles and angiotensin converting enzyme inhibition of milk protein concentrate hydrolysates

Uluko, Hankie; Lü, Ling; Li, Hongjuan; Cui, Wenming; Zhang, Shuwen; Zhao, Lili; Xue, Haixiao; Lv, Jing

doi:10.1002/jsfa.6572

Cited by 27 publications

(12 citation statements)

References 43 publications

(104 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Likewise, increasing the sonication time from 3 to 12 min gave rise to the DH from 16.24 to 22.07%. These results agree with previous studies where it was seen that sonication prior to enzymolysis increased the DH and the enzymolysis rate [36][37][38]. Similarly, the exposure time of sonication greatly increased the ACE inhibitory activity from 51.10 to 72.13%.…”

Section: Effect Of Ultrasonic Power and Time On Degree Of Hydrolysis supporting

confidence: 92%

Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

Wali

Shahnawaz

et al. 2017

Journal of Chemistry

View full text Add to dashboard Cite

The effects of power ultrasound pretreatments on the degree of hydrolysis (DH), angiotensin-I-converting enzyme (ACE) inhibitory activity, amino acid composition, surface hydrophobicity, protein solubility, and thermal stability of ACE inhibition of rapeseed protein hydrolysates were evaluated. Ultrasonic pretreatments before enzymolysis in terms of power and exposure time increased the DH and ACE inhibitory activities over the control (without sonication). In this study, maximum DH 22.07% and ACE inhibitory activity 72.13% were achieved at 600 W and 12 min pretreatment. Compared to the hydrolysates obtained without sonication, the amino acid profile of ultrasound pretreated hydrolysates showed significant changes particularly in the proline content and hydrophobic amino acids with an increased rate of 2.47% and 6.31%, respectively. Ultrasound pretreatment (600 watts, 12 min) improved functional properties of protein hydrolysates over control by enhancing surface hydrophobicity and solubility index with an increased rate of 130.76% and 34.22%. Moreover, the stability test showed that the ACE inhibitory activity remains stable against heat treatments. However, extensive heat, prolonged heating time, and alkaline conditions were not in the favor of stability test, while under mild heat and acidic conditions their ACE inhibitory activities were not significantly different from unheated samples.

show abstract

Section: Effect Of Ultrasonic Power and Time On Degree Of Hydrolysis supporting

confidence: 92%

Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

Wali

Shahnawaz

et al. 2017

Journal of Chemistry

View full text Add to dashboard Cite

show abstract

“…Uluko et al . () have considered that activity increase resulted from the production of new small peptides. But little systematic analysis is provided from previous studies.…”

Section: Introductionmentioning

confidence: 97%

“…Most of plant protein isolates contain denatured proteins, due to the commonly applied industrial processes (Joshi et al ., ; Liu et al ., ,b), which lead to the traditional enzymolysis has many drawbacks such as low conversion rate of the substrate, longer reaction time and high energy consumption (Qu et al ., ). Thus, some pretreatment technologies as ultrasound (Jia et al ., ; Qu et al ., ; Uluko et al ., ; Jin et al ., ,b), high hydrostatic pressure (Quirós et al ., ; Zhang et al ., ), heat treatment (Zhang et al ., ), microwave (Izquierdo et al ., ), extrusion (Wang et al ., ) and pulsed electric field (Toepfl et al ., ) have been used to enhance the hydrolysis of proteins.…”

Section: Introductionmentioning

confidence: 99%

“…Antihypertensive is an important activity that the protein hydrolysates referred to. Some of the studies have indicated that protein pretreatment can increase ACE inhibitory activity of hydrolysates (Quir os et al, 2007;Jia et al, 2010;Zhang et al, 2013;Uluko et al, 2014). A few studies have discussed the reason resulted from protein pretreatment.…”

Section: Introductionmentioning

confidence: 99%

“…Jia et al (2010) have concluded that ultrasonic pretreatment could accelerate the release of hydrophobic amino acid. Uluko et al (2014) have considered that activity increase resulted from the production of new small peptides. But little systematic analysis is provided from previous studies.…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

High‐pressure microfluidisation pretreatment disaggregate peanut protein isolates to prepare antihypertensive peptide fractions

Gong

Deng

Shi

et al. 2017

Int J of Food Sci Tech

View full text Add to dashboard Cite

Summary High‐pressure microfluidisation (HPM) pretreatment was applied to increase in vitro antihypertensive activity of peanut peptide fractions (PPF). The morphology of protein in aqueous dispersion revealed that peanut protein isolate (PPI) disaggregated at relatively low pressure (≤120 MPa) and re‐aggregated at relatively high pressures (150–210 MPa). The treated pressure of 120 MPa could lead to the most disaggregation of PPI. Small peptides contents, trichloroacetic acid‐nitrogen soluble index (TCA‐NSI) and degree of hydrolysis (DH) of peanut protein hydrolysates (PPH) all reached the highest at 120 MPa. Consequently, it possessed the highest angiotensin converting enzyme (ACE) and renin inhibitory activity. The highest surface hydrophobicity occurred at 120 MPa pretreatment samples. Thirty‐nine oligopeptides at 120 MPa pretreatment were identified by ultra‐performance liquid chromatography‐quadrupole time‐of‐flight (UPLC‐Q‐TOF) mass spectrometer combined with Progenesis QI for Proteomics software compared with 29 and 35 at control and 210 MPa, respectively. This meant that disaggregation of PPI at 120 MPa resulted in the release of new hydrophobic peptide.

show abstract

Separation and identification of antioxidant peptides from foxtail millet (Setaria italica) prolamins enzymatic hydrolysate

Feng

Mao

2019

Cereal Chem

View full text Add to dashboard Cite

Background and objectives Prolamins are the primary component of millet protein, constituting over 50% (w/w) of the total protein. This study aimed to prepare and identify bioactive peptides from millet prolamins (MP). Findings Ultrasonic and heat treatment could change the secondary structure conformation of the protein and invert part of the α‐helices into β‐sheets or β‐turns. After these treatments, the degree of hydrolysis increased. The alcalase‐hydrolyzed fraction with molecular weight <1 kDa exhibited the highest antioxidant activity. The bioactive peptides were separated and purified by gel‐filtration chromatography and reversed‐phase high‐performance liquid chromatography. Two novel peptides with molecular weights of 522.3 and 785.5 Da were identified as Pro‐Phe‐Leu‐Phe (PFLF) and Ile‐Ala‐Leu‐Leu‐Ile‐Pro‐Phe (IALLIPF), respectively. Both peptides showed high antioxidant activity, especially PFLF, the 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH) radical scavenging ability (RSA) of which was 149 μM TE/g protein, and the Oxygen radical absorbance capacity (ORAC) value reached 1,180 μM TE/g protein. Conclusions The results demonstrate that ultrasonic and heat treatment could enhance hydrolysis of MP by protease and antioxidant peptides with high DPPH RSA as well as ORAC value were purified and obtained. Significance and novelty Ultrasonic and heat treatment increased degree of MP hydrolysis. Two antioxidant peptides were successfully obtained from millet prolamins.

show abstract

Effect of power ultrasound pretreatment on peptidic profiles and angiotensin converting enzyme inhibition of milk protein concentrate hydrolysates

Abstract: Ultrasound pretreatment of MPC increases the ACE inhibitory activity of the hydrolysates because of the production of new small peptides. This can be used as a means to derive potent ACE inhibitory peptides at industrial scale in complex protein sources.

Cited by 27 publications

References 43 publications

Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

High‐pressure microfluidisation pretreatment disaggregate peanut protein isolates to prepare antihypertensive peptide fractions

Separation and identification of antioxidant peptides from foxtail millet (Setaria italica) prolamins enzymatic hydrolysate

Contact Info

Product

Resources

About