Effect of ultrasound pretreatment on structural, physicochemical, rheological and gelation properties of transglutaminase cross-linked whey protein soluble aggregates.

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Tytuł:: Effect of ultrasound pretreatment on structural, physicochemical, rheological and gelation properties of transglutaminase cross-linked whey protein soluble aggregates.
Autorzy:: Zhang T; Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Zhao Y; Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Tian X; Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Liu J; Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.
Ye H; Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China. Electronic address: .
Shen X; Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China. Electronic address: .
Źródło:: Ultrasonics sonochemistry [Ultrason Sonochem] 2021 Jun; Vol. 74, pp. 105553. Date of Electronic Publication: 2021 Apr 15.
Typ publikacji:: Journal Article
Język:: English
Imprint Name(s):: Publication: Amsterdam : Elsevier Science
Original Publication: Oxford : Butterworth Heinemann, c1994-
MeSH Terms:: Chemical Phenomena*
Protein Aggregates*
Rheology*
Ultrasonic Waves*
Transglutaminases/*metabolism
Gels ; Solubility
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Contributed Indexing:: Keywords: Gelation property; High intensity ultrasound; Rheological property; Transglutaminase; Whey protein soluble aggregates
Substance Nomenclature:: 0 (Gels)
0 (Protein Aggregates)
EC 2.3.2.13 (Transglutaminases)
Entry Date(s):: Date Created: 20210423 Date Completed: 20210816 Latest Revision: 20231111
Update Code:: 20240104
PubMed Central ID:: PMC8091057
DOI:: 10.1016/j.ultsonch.2021.105553
PMID:: 33892260
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A solution (10%, w/v) of whey protein soluble aggregates (WPISA) was pretreated with high-intensity ultrasound (HUS, 20 kHz) for different durations (10-40 min) before incubation with transglutaminase (TGase) to investigate the effect of HUS on the structural, physicochemical, rheological, and gelation properties of TGase cross-linked WPISA. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) results showed that HUS increased the amounts of high-molecular-weight polymers/aggregates in WPISA after incubation with TGase. HUS significantly increased (P < 0.05) the degree of TGase-mediated cross-linking in WPISA, as demonstrated by a reduction in free amino group contents. HUS significantly increased (P < 0.05) the particle size, intrinsic fluorescence intensity, and surface hydrophobicity of TGase cross-linked WPISA, but had no significant impact (P > 0.05) on the zeta-potential or total free sulfhydryl group content of TGase cross-linked WPISA. The apparent viscosity and the consistency index of TGase cross-linked WPISA were significantly increased by HUS (P < 0.05), which indicated that HUS facilitated the formation of more high-molecular-weight polymers. HUS significantly increased (P < 0.05) the water holding capacity and gel strength of glucono-δ-lactone (GDL)-induced TGase cross-linked WPISA gels. The results indicated that HUS could be an efficient tool for modifying WPISA to improve its degree of TGase-mediated cross-linking, which would lead to improved rheological and gelation properties.
(Copyright © 2021 The Authors. Published by Elsevier B.V. All rights reserved.)

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