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Zinc-binding behavior of hemp protein hydrolysates: Soluble versus insoluble zinc-peptide complexes
Journal of Functional Foods ( IF 5.6 ) Pub Date : 2018-08-20 , DOI: 10.1016/j.jff.2018.08.019
Qingling Wang , Youling L. Xiong

Proteins and peptides when forming complexes with zinc can increase zinc bioavailability. Such complexation was investigated on hemp protein hydrolysates (HPHs) in the present study using Pepsin, Alcalase, Flavourzyme, Papain, Protamex, and Trypsin. Two solubility fractions of Zn2+–HPH complexes, i.e., P1 (water-insoluble large peptides) and P2 (water-soluble small peptides, precipitable by ethanol), were collected. The FTIR analysis on Pepsin-HPH suggested that P1 and P2 peptides had different Zn2+-binding sites where NH and CO were the primary sites in P1 and P2, respectively. Although the Zn2+-binding capacity (P1 and P2 combined) of HPHs was lower than that of nonhydrolyzed hemp protein, the P2-bound Zn2+ was more abundant in HPHs (up to 63.4%) than in nonhydrlyzed protein (29.6%). Isothermal titration calorimetry corroborated with Zn2+-binding capacity for different HPH samples. Peptides produced with Flavourzyme had the highest Zn2+-binding activity (88.8%) while those with Pepsin exhibited the maximum solubility.



中文翻译:

大麻蛋白水解产物的锌结合行为:可溶性与不溶性锌肽复合物

与锌形成复合物时,蛋白质和肽可以增加锌的生物利用度。在本研究中,使用胃蛋白酶,Alcalase,Flavourzyme,木瓜蛋白酶,Protamex和胰蛋白酶对大麻蛋白水解物(HPHs)进行了研究。收集了Zn 2+ –HPH络合物的两个溶解度分数,即P 1(水不溶性大肽)和P 2(水溶性小肽,可被乙醇沉淀)。对胃蛋白酶-HPH的FTIR分析表明,P 1和P 2肽具有不同的Zn 2+结合位点,其中N H和C O分别是P 1和P 2中的主要位点。虽然锌HPHs的2+结合能力(结合的P 1和P 2)低于未水解的大麻蛋白,HPHs中的P 2结合的Zn 2+比未水解的蛋白(29.6%)更丰富(高达63.4%) )。等温滴定量热法证实了对不同HPH样品的Zn 2+结合能力。用Flavourzyme生产的肽具有最高的Zn 2+结合活性(88.8%),而使用胃蛋白酶的肽则具有最大的溶解度。

更新日期:2018-08-20
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