Effect of ultrasonic pretreatment on whey protein hydrolysis by alcalase: Thermodynamic parameters, physicochemical properties and bioactivities. (April 2018)
- Record Type:
- Journal Article
- Title:
- Effect of ultrasonic pretreatment on whey protein hydrolysis by alcalase: Thermodynamic parameters, physicochemical properties and bioactivities. (April 2018)
- Main Title:
- Effect of ultrasonic pretreatment on whey protein hydrolysis by alcalase: Thermodynamic parameters, physicochemical properties and bioactivities
- Authors:
- Wu, Qiongying
Zhang, Xuefen
Jia, Junqiang
Kuang, Cong
Yang, Hongshun - Abstract:
- Graphical abstract: Highlights: E a, Δ H and Δ S Values for whey protein enzymolysis were decreased by ultrasound. Ultrasound led to changes in physicochemical properties of whey protein. Bioactivities of whey protein hydrolysates were increased by ultrasound. Ultrasonic pretreatment can improve the efficiency of whey protein hydrolysis. Abstract: The effects of ultrasonic pretreatment on the enzymolysis thermodynamics and physicochemical properties of whey protein, and the mechanisms behind those effects, were investigated. Changes in the angiotensin-I converting enzyme (ACE) inhibitory and immunomodulatory activities of whey protein hydrolysates after ultrasonic pretreatment were also determined. Results showed that the ultrasonicated whey protein had a higher in degree of hydrolysis than the non-sonicated protein. After the pretreatment, the activation energy ( E a ), enthalpy of activation (Δ H ) and entropy of activation (Δ S ) of whey protein enzymolysis were decreased by 15.9%, 16.8%, and 16.4%, respectively. There was no significant change in free energy (Δ G ) ( P > 0.05). Physicochemical analysis revealed that ultrasound had induced unfolding of the whey protein, resulting in a 43.7% increase in its surface free sulfhydryl content and a 62.6% increase in surface hydrophobicity. Ultrasound significantly decreased the protein's α-helical content and significantly increased its β-sheets and β-turns ( P < 0.05). The ACE inhibitory and immunomodulatory activities ofGraphical abstract: Highlights: E a, Δ H and Δ S Values for whey protein enzymolysis were decreased by ultrasound. Ultrasound led to changes in physicochemical properties of whey protein. Bioactivities of whey protein hydrolysates were increased by ultrasound. Ultrasonic pretreatment can improve the efficiency of whey protein hydrolysis. Abstract: The effects of ultrasonic pretreatment on the enzymolysis thermodynamics and physicochemical properties of whey protein, and the mechanisms behind those effects, were investigated. Changes in the angiotensin-I converting enzyme (ACE) inhibitory and immunomodulatory activities of whey protein hydrolysates after ultrasonic pretreatment were also determined. Results showed that the ultrasonicated whey protein had a higher in degree of hydrolysis than the non-sonicated protein. After the pretreatment, the activation energy ( E a ), enthalpy of activation (Δ H ) and entropy of activation (Δ S ) of whey protein enzymolysis were decreased by 15.9%, 16.8%, and 16.4%, respectively. There was no significant change in free energy (Δ G ) ( P > 0.05). Physicochemical analysis revealed that ultrasound had induced unfolding of the whey protein, resulting in a 43.7% increase in its surface free sulfhydryl content and a 62.6% increase in surface hydrophobicity. Ultrasound significantly decreased the protein's α-helical content and significantly increased its β-sheets and β-turns ( P < 0.05). The ACE inhibitory and immunomodulatory activities of the whey protein hydrolysates were significantly increased by ultrasonic pretreatment ( P < 0.05). These results suggest that ultrasound can be applied to enhance whey protein enzymolysis for the generation of novel bioactive peptides that can be used as drug or functional food ingredient. … (more)
- Is Part Of:
- Process biochemistry. Volume 67(2018)
- Journal:
- Process biochemistry
- Issue:
- Volume 67(2018)
- Issue Display:
- Volume 67, Issue 2018 (2018)
- Year:
- 2018
- Volume:
- 67
- Issue:
- 2018
- Issue Sort Value:
- 2018-0067-2018-0000
- Page Start:
- 46
- Page End:
- 54
- Publication Date:
- 2018-04
- Subjects:
- DH degree of hydrolysis -- ACE angiotensin-І converting enzyme -- DTNB 5, 5′-Dithiobis(2-nitrobenzoic acid) -- ANS 1-anilino-8-naphthalene sulfonate -- HHL Hippuryl-His-Leu -- MTT 3-(4, 5-dimethylthiazol-2-yl) -2, 5-diphenyltetrazolium bromide -- DMSO dimethyl sulfoxide -- FBS Fetal bovine serum -- kin effective (total) rate constant -- A pre-exponential or collision factor -- R universal gas constant -- T Kelvin temperature -- kB Boltzmann constant -- h Planck constant -- Ea activation energy -- Δ SSentropy of activation -- ΔG free energies of activation -- ΔH enthalpy of activation -- SH sulfhydryl
Whey protein -- Ultrasound -- Thermodynamics -- Physicochemical properties -- ACE inhibitory -- Immunomodulatory
Biochemical engineering -- Periodicals
Biotechnology -- Periodicals
Biochemistry -- periodicals
Biotechnology -- periodicals
Chemical Engineering -- periodicals
Génie biochimique -- Périodiques
Biotechnologie -- Périodiques
Biochemical engineering
Biotechnology
Periodicals
660.63 - Journal URLs:
- http://www.sciencedirect.com/science/journal/13595113 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.procbio.2018.02.007 ↗
- Languages:
- English
- ISSNs:
- 1359-5113
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6849.983500
British Library DSC - BLDSS-3PM
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- 6421.xml