Phosvitin(PV)is a highly phosphorylated protein found in egg yolk.PV hydrolysate(PPP)has excellent calciumbinding capacity,although its ability to promote calcium deposition and the underlying mechanism are unclear.Th...Phosvitin(PV)is a highly phosphorylated protein found in egg yolk.PV hydrolysate(PPP)has excellent calciumbinding capacity,although its ability to promote calcium deposition and the underlying mechanism are unclear.This study aimed to explore the calcium deposition capacity and mechanisms of PPP and PPP-Ca.The fraction 3(PPP3)was isolated by anion-exchange chromatography and exhibited the best calcium-binding activity(98.11±0.91%).To mimic the microenvironment of bone formation,a three-cell co-culture model of intestinal epithelial cells-osteoblasts-osteoclasts(Caco-2/MC3T3-E1/RAW264.7)was established.The alkaline phosphatase results indicated that PPP3 and PPP3-Ca significantly promoted osteoblasts differentiation compared to CaCl_(2).Correspondingly,PPP3,PPP3-Ca,and CaCl_(2) reduced tartrate resistant acid phosphatase content by 43.84%,46.92% and 17.21%,respectively,suggesting that PPP3 and PPP3-Ca effectively inhibited osteoclasts differentiation.The molecular mechanism by which PPP3 and PPP3-Ca inhibited osteoclasts bone resorption involved regulating mRNA expression of the OPG/RANKL/RANK pathway.Notably,PPP3-Ca demonstrated higher pro-calcium deposition in co-cultured cells,about 1.70 times higher than CaCl_(2).PPP3-Ca dependent high phosphorylation exerted a pro-mineralization effect,as analyzed by scanning electron microscopy and energy dispersive spectroscopy.Overall,this study suggested that PPP3-Ca as organic calcium was more effective than CaCl_(2) in promoting calcium deposition.展开更多
The aim of this study was to investigate the structure and stability of silver carp skin collagen peptide-calcium chelate(SSCPs-Ca)and evaluate its effectiveness in promoting calcium absorption.SSCPs were prepared by ...The aim of this study was to investigate the structure and stability of silver carp skin collagen peptide-calcium chelate(SSCPs-Ca)and evaluate its effectiveness in promoting calcium absorption.SSCPs were prepared by twostep enzymatic hydrolysis and chelated with calcium to form SSCPs-Ca.The structure of SSCPs-Ca was characterized by ultra-violet spectroscopy,fluorescence spectroscopy,particle size distribution,scanning electron microscopy and atomic force microscopy.Then explored the effects of temperature,lactose,sodium chloride and phosphate on its stability.The calcium uptake of SSCPs-Ca was evaluated using Caco-2 cell and zebrafish osteoporosis models.Compared to SSCPs,SSCPs-Ca exhibited notable improvements in particle size and adopted a stable,osteocalcin-like crystal structure.SSCPs-Ca exhibited enhanced electrostatic repulsion and thermal stability.SSCPs-Ca significantly enhanced calcium transport and absorption at the cellular level,outperforming CaCl2.Unlike traditional supplements,its efficiency remained unaffected by dietary components such as lactose and NaCl.SSCPs-Ca operated independently of Vitamin D for calcium transport,emphasizing its innovative mechanism.SSCPs-Ca at a concentration of 125μg/mL demonstrated superior efficacy in mitigating osteoporosis in zebrafish models,achieving comparable results to etidronate disodium at a concentration of 300μg/mL.These findings established SSCPs-Ca as a groundbreaking calcium supplement with the potential to significantly improve bone health.By addressing calcium deficiency and associated risks with enhanced bioavailability and stability,SSCPs-Ca offered a promising alternative to traditional calcium supplements,paving the way for innovative strategies in managing calcium-related health challenges.展开更多
基金financially supported by the National Natural Science Foundation of China(grant number 32072237)Shandong Prov-ince Science and Technology-based Smalland Medium-sized Enterprises Innovation Capacity Enhancement Project(grant number 2023TSGC0934)earmarked fund for Hebei Agriculture Research System(HBCT2024260208).
文摘Phosvitin(PV)is a highly phosphorylated protein found in egg yolk.PV hydrolysate(PPP)has excellent calciumbinding capacity,although its ability to promote calcium deposition and the underlying mechanism are unclear.This study aimed to explore the calcium deposition capacity and mechanisms of PPP and PPP-Ca.The fraction 3(PPP3)was isolated by anion-exchange chromatography and exhibited the best calcium-binding activity(98.11±0.91%).To mimic the microenvironment of bone formation,a three-cell co-culture model of intestinal epithelial cells-osteoblasts-osteoclasts(Caco-2/MC3T3-E1/RAW264.7)was established.The alkaline phosphatase results indicated that PPP3 and PPP3-Ca significantly promoted osteoblasts differentiation compared to CaCl_(2).Correspondingly,PPP3,PPP3-Ca,and CaCl_(2) reduced tartrate resistant acid phosphatase content by 43.84%,46.92% and 17.21%,respectively,suggesting that PPP3 and PPP3-Ca effectively inhibited osteoclasts differentiation.The molecular mechanism by which PPP3 and PPP3-Ca inhibited osteoclasts bone resorption involved regulating mRNA expression of the OPG/RANKL/RANK pathway.Notably,PPP3-Ca demonstrated higher pro-calcium deposition in co-cultured cells,about 1.70 times higher than CaCl_(2).PPP3-Ca dependent high phosphorylation exerted a pro-mineralization effect,as analyzed by scanning electron microscopy and energy dispersive spectroscopy.Overall,this study suggested that PPP3-Ca as organic calcium was more effective than CaCl_(2) in promoting calcium deposition.
基金supported by China Agriculture Research System(Program No.CARS-45-27).
文摘The aim of this study was to investigate the structure and stability of silver carp skin collagen peptide-calcium chelate(SSCPs-Ca)and evaluate its effectiveness in promoting calcium absorption.SSCPs were prepared by twostep enzymatic hydrolysis and chelated with calcium to form SSCPs-Ca.The structure of SSCPs-Ca was characterized by ultra-violet spectroscopy,fluorescence spectroscopy,particle size distribution,scanning electron microscopy and atomic force microscopy.Then explored the effects of temperature,lactose,sodium chloride and phosphate on its stability.The calcium uptake of SSCPs-Ca was evaluated using Caco-2 cell and zebrafish osteoporosis models.Compared to SSCPs,SSCPs-Ca exhibited notable improvements in particle size and adopted a stable,osteocalcin-like crystal structure.SSCPs-Ca exhibited enhanced electrostatic repulsion and thermal stability.SSCPs-Ca significantly enhanced calcium transport and absorption at the cellular level,outperforming CaCl2.Unlike traditional supplements,its efficiency remained unaffected by dietary components such as lactose and NaCl.SSCPs-Ca operated independently of Vitamin D for calcium transport,emphasizing its innovative mechanism.SSCPs-Ca at a concentration of 125μg/mL demonstrated superior efficacy in mitigating osteoporosis in zebrafish models,achieving comparable results to etidronate disodium at a concentration of 300μg/mL.These findings established SSCPs-Ca as a groundbreaking calcium supplement with the potential to significantly improve bone health.By addressing calcium deficiency and associated risks with enhanced bioavailability and stability,SSCPs-Ca offered a promising alternative to traditional calcium supplements,paving the way for innovative strategies in managing calcium-related health challenges.
