JOURNAL OF FOOD BIOCHEMISTRY
·
2014
·Vol. 38
·期 3
·374-380
·
IF 0.853
Mei-Ling Zhang,Xin-Huai Zhao
Soy protein hydrolysate (SPH) (1 mg/mL), generated by alcalase, had a calcium-chelating activity of 41 mg/g peptide. The alcalase-catalyzed plastein reaction of SPH was carried out in different media: ethanol–water, methanol–water and water. The effects of SPH and of resulting modified hydrolysates on calcium-chelating activities and inhibition of calcium precipitation and platelet aggregation were assessed in vitro . The optimum ethanol concentration, alcalase level and reaction temperature for the plastein reaction was 56.8% v/v, 5.26 kU/g peptide and 33.1C, respectively. The modified hydrolysates had better calcium-chelating activities and stronger inhibition of calcium precipitation and platelet aggregation than SPH. The modified hydrolysate with the highest calcium-chelating activity showed the strongest inhibitory effects on platelet aggregation and calcium precipitation. The plastein reaction enhances the in vitro calcium-chelating and platelet anti-aggregation activities of SPH. Practical Applications In this study, an alcalase-catalyzed plastein reaction carried out in three media (ethanol–water, methanol–water and water) was used to modify the in vitro calcium-chelating and platelet anti-aggregation activities of an alcalase-generated soy protein hydrolysate. The results revealed that the modified hydrolysates of higher calcium-chelating activity had stronger inhibitory effects on platelet aggregation and calcium precipitation. The results of this study provide further insight on the enzymatic synthesis of bioactive peptides of higher activity using the plastein reaction.
研究领域:
食品科学
·
生物化学
✓ 已验证
产品关联
DOI
高影响因子
Food and Bioprocess Technology
·
2024
·Vol. 17
·期 11
·3693-3703
·
IF 5.3
Xu Chengzhi,Cai Chaonan,Liu Tianyi,Kang Jizhen,Li Sheng,Zhang Juntao,Wei Benmei,Wang Haibo
An important area of focus for developing antioxidant collagen hydrolysates (peptides) involves enhancing the antioxidant properties of collagen hydrolysates. In this study, fish scale collagen hydrolysate (FH) was used as the raw material for plastein reaction. Various enzymes, including papain, alcalase, flavourzyme, and the combination of alcalase and flavourzyme, were employed for this purpose. The plastein reaction significantly improved the thermal stability, chemical antioxidant activity, and capacity to scavenge cellular reactive oxygen species of FH. Notably, the plastein reaction catalyzed by alcalase exhibited the most significant improvement, increasing the hydroxyl radical scavenging rate from 72.3 to 93.4% and restoring the viability of the oxidative stress-induced HepG2 cell model from 50.8 ± 1.7 to 74.9 ± 1.7%. During the plastein reaction, condensation and hydrolysis reactions occurred simultaneously, with condensation being the dominant process. These reactions, along with physical aggregation, facilitated the formation of larger yet more concentrated collagen peptide aggregates, leading to increased exposure of hydrophobic groups. This enhanced the uptake of collagen hydrolysates by the cells and contributed to the enhancement of their antioxidant properties. Thus, the plastein reaction is an effective method for enhancing the antioxidant properties of collagen hydrolysates, with its simplicity of operation and promising application potential.
研究领域:
食品科学
·
生物化学
·
生物技术
·
海洋生物技术
·
药学
✓ 已验证
DOI
高影响因子
ACS Food Science & Technology
·
2025
·
IF 2.8
Yun-Jiao Shi,Hua-Qiang Li,Xin-Huai Zhao
The hydrolysate of salmon skin gelatin (HSSG) was generated by hydrolyzing salmon skin gelatin with papain and then modified using a papain-catalyzed plastein reaction with or without one of the three exogenous Gly, Pro, and Hyp. The prepared samples including HSSG, the HSSG modifier alone (namely, PHSSG), three HSSG modifiers with one of the exogenous amino acids (namely, PHSSG-Gly, PHSSG-Pro, and PHSSG-Hyp), and three mixtures of HSSG plus one of the exogenous amino acids (namely, HSSG-Gly, HSSG-Pro, and HSSG-Hyp) were thus assessed for their activities toward the lipopolysaccharide (LPS)-stimulated RAW264.7 macrophages. These samples were all nontoxic to the macrophages but showed different abilities to promote cell growth. LPS promoted macrophage phagocytosis and lactate dehydrogenase release and enhanced the production levels of intracellular reactive oxygen species, NO, prostaglandin E2, and four inflammatory cytokines including TNF-α, IL-6, TGF-β1, and IL-10. Meanwhile, HSSG, PHSSG, and PHSSG-Hyp alleviated the LPS-induced macrophage inflammation by regulating the expression of 12 inflammation-related genes including iNOS, IL-6, TNF-α, IL-1β, COX-2, TLR4, IL-10, TGF-β1, miR-181a, miR-30d, miR-155, and miR-148a, downregulating the expression of five proteins including p-NF-κB-p65, MyD88, p-IKKα, p-IκBα, and iNOS that are associated with cell inflammation and reducing the nuclear translocation of p65 in the nucleus. Among the three evaluated samples, PHSSG-Hyp and HSSG had the respective highest and lowest anti-inflammatory activities in the LPS-induced macrophages via inactivating the NF-κB signaling pathway. It was thus concluded that the plastein reaction used in the presence of Hyp endowed HSSG with the highest anti-inflammatory activity in the macrophages, highlighting the potential use of this reaction in protein hydrolysates to reach activity enhancement and to produce functional peptide products.
研究领域:
生物化学
·
免疫学
·
食品科学
✓ 已验证
产品关联
DOI
高影响因子
危险品化学品经营许可证（带存储）