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超声预处理对转谷氨酰胺酶交联乳清蛋白可溶性聚集物结构、理化、流变和胶凝特性的影响。

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

机构信息

Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.

Department of Food Science, College of Food Science and Engineering, Jilin University, Changchun 130062, China.

出版信息

Ultrason Sonochem. 2021 Jun;74:105553. doi: 10.1016/j.ultsonch.2021.105553. Epub 2021 Apr 15.

DOI:10.1016/j.ultsonch.2021.105553
PMID:33892260
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8091057/
Abstract

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.

摘要

乳清蛋白可溶聚集物(WPISA)的 10%(w/v)溶液先经过高强度超声(HUS,20 kHz)处理不同时间(10-40 分钟),然后再与转谷氨酰胺酶(TGase)孵育,以研究 HUS 对 TGase 交联 WPISA 的结构、物理化学、流变和胶凝特性的影响。十二烷基硫酸钠聚丙烯酰胺凝胶电泳(SDS-PAGE)结果表明,HUS 增加了 WPISA 与 TGase 孵育后高分子量聚合物/聚集物的数量。HUS 显著增加(P < 0.05)了 WPISA 中 TGase 介导的交联程度,这表现在游离氨基含量的减少。HUS 显著增加(P < 0.05)了 TGase 交联 WPISA 的粒径、内源荧光强度和表面疏水性,但对 TGase 交联 WPISA 的 Zeta 电位或总游离巯基含量没有显著影响(P > 0.05)。HUS 显著增加(P < 0.05)了 TGase 交联 WPISA 的表观黏度和稠度指数,这表明 HUS 促进了更多高分子量聚合物的形成。HUS 显著增加(P < 0.05)了戊二醛(GDL)诱导的 TGase 交联 WPISA 凝胶的持水能力和凝胶强度。结果表明,HUS 可以作为一种有效的工具来修饰 WPISA,以提高其 TGase 介导的交联程度,从而改善流变和胶凝特性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/2f0f34ac4885/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/3921575b4d85/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/33d1d74fd4cd/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/9ecd8b890ff6/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/d2a554bc42cb/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/877b09d8707e/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/23b9431382c3/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/2f0f34ac4885/gr6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/3921575b4d85/ga1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/33d1d74fd4cd/gr1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/9ecd8b890ff6/gr2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/d2a554bc42cb/gr3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/877b09d8707e/gr4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/23b9431382c3/gr5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/779d/8091057/2f0f34ac4885/gr6.jpg

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