Gelation and microstructural properties of protein hydrolysates from trypsin-treated male gonad of scallop (Patinopecten yessoensis) modified by kappa-Carrageenan/K

Gelation and microstructural properties of protein hydrolysates from trypsin-treated male gonad of scallop (Patinopecten yessoensis) modified by kappa-Carrageenan/K
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kappa-卡拉胶/K 修饰的扇贝(虾夷扇贝)雄性性腺胰蛋白酶处理蛋白水解物的凝胶化和微观结构特性

DOI:
10.1016/j.foodhyd.2019.01.024
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发表时间:
2019
期刊:
影响因子:
10.7
通讯作者:
Zhu Bei-Wei
Zhu Bei-Wei
中科院分区:
农林科学1区
文献类型:
--
作者:
Yan Jia-Nan;Shang Wen-Hui;Zhao Jun;Han Jia-Run;Jin Wen-Gang;Wang Hai-Tao;Du Yi-Nan;Wu Hai-Tao;Janaswamy Srinivas;Xiong Youling L;Zhu Bei-Wei

文献摘要

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研究了扇贝雄性性腺水解物(SMGHs)在κ-卡拉胶(κ-C)存在下,经氯化钾(KCl)处理和未处理后的凝胶特性和微观结构特征。κ-C的存在显著提高了SMGH的弹性模量(10.3-449.5 Pa)和熔融温度(32.7-46.7 °C)。弛豫时间(T21,T23)的减少表明SMGH与κ-C之间的强结合。酰胺I和II峰的蓝移,加上SMGH/κ-C中1159 cm− 1的新谱带,进一步证明了SMGH和κ-C之间的静电相互作用。κ-C使SMGH的β-折叠比例从28.10%上升到35.93%,但α-螺旋和β-转角比例下降,内源性荧光明显减弱。这种情况导致更紧密的网络形成和κ-C链的絮凝。对κ-C的盐处理促进了螺旋的形成,然而,SMGH的存在由于SMGH的聚集而在κ-C网络中产生了更大的间隙空间,并降低了整体凝胶强度。这一结果为基于蛋白质和多糖复合物的功能性水凝胶的设计和开发提供了新的机会,可用于食品,制药和生物医学应用。
This article reported the gelation and microstructural properties of scallop male gonads hydrolysates (SMGHs) in the presence of κ-Carrageenan (κ-C) and treated or untreated with potassium chloride (KCl). The presence of κ-C significantly increased the elastic moduli (10.3–449.5 Pa) and melting temperature (32.7–46.7 °C) of SMGHs. The decrease in the relaxation time (T21, T23) signified the strong binding between SMGHs and κ-C. The blue shift in the amide I and II peals coupled with a new band of 1159 cm−1in SMGHs/κ-C further demonstrated the electrostatic interactions between SMGHs and κ-C. κ-C rose the percentage of β-sheets from 28.10% to 35.93% but at the expense of α-helix and β-turn fractions and highly ebbed the intrinsic fluorescence of SMGHs. Such scenarios resulted in a more compact network formation and flocculation of κ-C chains. The salt-treatment to κ-C promoted helical formation, however, presence of SMGHs created larger interstitial spaces in the κ-C network due to aggregates of SMGHs and decreased the overall gel strength. The outcome promises novel opportunities in the design and development of functional hydrogels based on protein and polysaccharide complexes for food, pharmaceutical and biomedical applications.