Huiying Wang
Current Organizations / Institutes
The organizations/institutes from the scholar's latest article
Huiying Wang has a total of 12 co-authors. Here are the top co-authors by number of shared publications:
- Wenhui Wu
Department of Marine Pharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China
3 shared publications - Haoze Yang
Department of Marine Biopharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China
2 shared publications - Jeevithan Elango
Department of Biomaterials Engineering, Faculty of Health Sciences, UCAM—Universidad Católica San Antonio de Murcia, Campus de los Jerónimos 135, Guadalupe, 30107 Murcia, Spain
2 shared publications - Qian Yao
Department of Marine Biopharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China
2 shared publications - Xiaozhen Diao
Department of Marine Pharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China
2 shared publications - Bailin Li
College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China
1 shared publication
Latest Publications
- Open Access
Gel Filtration Chromatography-Guided Sequential Hydrolysis of Sthenoteuthisoualaniensis Protein: Peptide Distribution and Functional Properties
The compact muscle architecture and poor aqueous dispersibility of Sthenoteuthis oualaniensis protein limit its use as a food ingredient. This study developed a gel filtration chromatography (GFC)-guided papain–alcalase sequential hydrolysis strategy using target-window peak area () as a peptide-distribution response. Box–Behnken optimization identified an enzyme dosage of 1110 U/g, a papain/alcalase mass ratio of 3:5, and 8 h hydrolysis, yielding an of 0.0648 ± 0.0012 a.u. O-phthaldialdehyde (OPA)-derived degree of hydrolysis (DH) values were 10.72 ± 0.08%, 35.32 ± 0.12%, and 25.03 ± 0.37% for SPH-Pap, SPH-Alc, and SPH-opt, respectively, showing that the highest did not coincide with the highest DH. The essential-to-total amino acid ratio remained 38.18–39.20%, while lysine and methionine changed modestly. SPH-opt maintained high solubility across a broad pH range and exhibited a peptide profile distinct from those of the single-enzyme hydrolysates. Radical-scavenging capacity was assessed only post-optimization. At 5 mg/mL, SPH-opt showed DPPH and ABTS scavenging rates of 23.75% and 22.84%, respectively; without external standards, these values support only relative within-study comparisons. Overall, and DH provided complementary information on peptide distribution and bond cleavage, and no causal relationship between and radical-scavenging capacity was established.Open AccessGel Filtration Chromatography-Guided Sequential Hydrolysis of Sthenoteuthisoualaniensis Protein: Peptide Distribution and Functional Properties
The compact muscle architecture and poor aqueous dispersibility of Sthenoteuthis oualaniensis protein limit its use as a food ingredient. This study developed a gel filtration chromatography (GFC)-guided papain–alcalase sequential hydrolysis strategy using target-window peak area () as a peptide-distribution response. Box–Behnken optimization identified an enzyme dosage of 1110 U/g, a papain/alcalase mass ratio of 3:5, and 8 h hydrolysis, yielding an of 0.0648 ± 0.0012 a.u. O-phthaldialdehyde (OPA)-derived degree of hydrolysis (DH) values were 10.72 ± 0.08%, 35.32 ± 0.12%, and 25.03 ± 0.37% for SPH-Pap, SPH-Alc, and SPH-opt, respectively, showing that the highest did not coincide with the highest DH. The essential-to-total amino acid ratio remained 38.18–39.20%, while lysine and methionine changed modestly. SPH-opt maintained high solubility across a broad pH range and exhibited a peptide profile distinct from those of the single-enzyme hydrolysates. Radical-scavenging capacity was assessed only post-optimization. At 5 mg/mL, SPH-opt showed DPPH and ABTS scavenging rates of 23.75% and 22.84%, respectively; without external standards, these values support only relative within-study comparisons. Overall, and DH provided complementary information on peptide distribution and bond cleavage, and no causal relationship between and radical-scavenging capacity was established. - Open Access
Isolationof PASN from Argentine Squid Carcass By-Products Enhances Proliferation and Repair of hACs and PC12 In Vitro via Antioxidant Activity
Marine by-products represent a promising source of bioactive peptides. This study aimed to isolate and characterize a low-molecular-weight peptide fraction with antioxidant activity from Argentine shortfin squid carcass by-products, and to evaluate in vitro its cytocompatibility and protective effects against corticosterone (CORT)-induced oxidative injury in rat adrenal pheochromocytoma (PC12) cells and human astrocyte (hACs) cells. Argentine squid antioxidant peptide (PASN) was obtained by size-exclusion chromatography and fractionation-based screening. PASN exhibited the strongest overall free-radical-scavenging activity and consisted predominantly of components below 1 kDa (211.73–1013.48 Da). Spectroscopic analyses indicated that enzymatic hydrolysis transformed its structure from a rigid triple-helix conformation to a more flexible conformation dominated by β-turns (50.78%) and random coils (17.38%). In addition, thermogravimetric analysis confirmed its excellent thermal stability, with an onset decomposition temperature as high as 244.81 °C, supporting its potential applicability in high-temperature food-processing matrices. In vitro assays demonstrated that PASN exhibited high biocompatibility and promoted proliferation of both PC12 cells and hACs, while significantly improving cell viability under CORT challenge. PASN also reduced lactate dehydrogenase (LDH) leakage (hACs: 38.31%; PC12: 31.17%) in both cell models and restored total superoxide dismutase (T-SOD) activity (hACs: 69.46%, PC12: 66.40%). Immunofluorescence further revealed that PASN rescued the expression of brain-derived neurotrophic factor (BDNF) (hACs: 35.23%, PC12: 12.50%) and glutamate decarboxylase (GAD1/2) (hACs: 102.66%, PC12: 31.31%), key markers associated with synaptic plasticity and GABAergic sleep regulation. Collectively, PASN is a thermally stable squid-derived peptide fraction that exerts antioxidant and cytoprotective effects in neural cell models in vitro and represents a promising sustainable candidate for nutraceutical development.
Open AccessIsolationof PASN from Argentine Squid Carcass By-Products Enhances Proliferation and Repair of hACs and PC12 In Vitro via Antioxidant Activity
Marine by-products represent a promising source of bioactive peptides. This study aimed to isolate and characterize a low-molecular-weight peptide fraction with antioxidant activity from Argentine shortfin squid carcass by-products, and to evaluate in vitro its cytocompatibility and protective effects against corticosterone (CORT)-induced oxidative injury in rat adrenal pheochromocytoma (PC12) cells and human astrocyte (hACs) cells. Argentine squid antioxidant peptide (PASN) was obtained by size-exclusion chromatography and fractionation-based screening. PASN exhibited the strongest overall free-radical-scavenging activity and consisted predominantly of components below 1 kDa (211.73–1013.48 Da). Spectroscopic analyses indicated that enzymatic hydrolysis transformed its structure from a rigid triple-helix conformation to a more flexible conformation dominated by β-turns (50.78%) and random coils (17.38%). In addition, thermogravimetric analysis confirmed its excellent thermal stability, with an onset decomposition temperature as high as 244.81 °C, supporting its potential applicability in high-temperature food-processing matrices. In vitro assays demonstrated that PASN exhibited high biocompatibility and promoted proliferation of both PC12 cells and hACs, while significantly improving cell viability under CORT challenge. PASN also reduced lactate dehydrogenase (LDH) leakage (hACs: 38.31%; PC12: 31.17%) in both cell models and restored total superoxide dismutase (T-SOD) activity (hACs: 69.46%, PC12: 66.40%). Immunofluorescence further revealed that PASN rescued the expression of brain-derived neurotrophic factor (BDNF) (hACs: 35.23%, PC12: 12.50%) and glutamate decarboxylase (GAD1/2) (hACs: 102.66%, PC12: 31.31%), key markers associated with synaptic plasticity and GABAergic sleep regulation. Collectively, PASN is a thermally stable squid-derived peptide fraction that exerts antioxidant and cytoprotective effects in neural cell models in vitro and represents a promising sustainable candidate for nutraceutical development.
- Open Access
- 23 February 2026
- Published by MDPI AG in Journal of Functional Biomaterials
- Vol. 17 (2) , 106
Construction of an In Vitro Blood–Brain Barrier Micro-Organoid Model Using Decellularized Squid Mantle Scaffold Film
Although blood–brain barrier (BBB) models are of great value in investigating neurological diseases, the structural complexity and intricate function based on cell–cell interactions of the BBB bring various limitations to the applications of existing models. In this study, a novel BBB micro-organoid model was established by culturing neurovascular unit (NVU) cells on a decellularized squid mantle scaffold (DSMS) film to reconstitute a more authentic and reliable NVU microenvironment for in vitro research. The DSMS applied was obtained from squid mantle scaffolds via decellularization, followed by defatting, and showed good biocompatibility with no cytotoxicity. The DSMS film was finally prepared by lyophilization. The lyophilized film exhibited a void ratio and pore size suitable for the adhesion and growth of endothelial cells (hCMEC/D3) and astrocytes (hACs), which led to the formation of a BBB-like spatial structure. The BBB micro-organoid model exhibited functional barrier properties, including an effective transendothelial electrical resistance (TEER) of approximately 230 Ω/cm2, restricted permeability to macromolecules—with apparent permeability coefficients (Papp) of 6.3 × 10−7 cm/s for 10 kDa and 2.7 × 10−7 cm/s for 70 kDa FITC–dextran—and expression of tight junctional complex (TJC) proteins such as vascular endothelial cadherin (VE-cad) and Zonula Occludens-1 (ZO-1). Furthermore, low-density lipoprotein receptor-related protein 1 (LRP1), a key receptor stably expressed in these two NVU cell types, was utilized as a critical indicator to assess the integrity of the BBB micro-organ model and its responsiveness to pathophysiological stimuli, particularly under thrombotic conditions. This study not only validates the feasibility of constructing a functionally competent BBB micro-organ model using DSMS films integrated with NVU cells but also provides a promising in vitro platform for subsequent studies on the BBB-related pathological mechanisms and the evaluation of drug permeability across the BBB.
- 23 February 2026
- Published by MDPI AG in Journal of Functional Biomaterials
- Vol. 17 (2) , 106
Open AccessConstruction of an In Vitro Blood–Brain Barrier Micro-Organoid Model Using Decellularized Squid Mantle Scaffold Film
Although blood–brain barrier (BBB) models are of great value in investigating neurological diseases, the structural complexity and intricate function based on cell–cell interactions of the BBB bring various limitations to the applications of existing models. In this study, a novel BBB micro-organoid model was established by culturing neurovascular unit (NVU) cells on a decellularized squid mantle scaffold (DSMS) film to reconstitute a more authentic and reliable NVU microenvironment for in vitro research. The DSMS applied was obtained from squid mantle scaffolds via decellularization, followed by defatting, and showed good biocompatibility with no cytotoxicity. The DSMS film was finally prepared by lyophilization. The lyophilized film exhibited a void ratio and pore size suitable for the adhesion and growth of endothelial cells (hCMEC/D3) and astrocytes (hACs), which led to the formation of a BBB-like spatial structure. The BBB micro-organoid model exhibited functional barrier properties, including an effective transendothelial electrical resistance (TEER) of approximately 230 Ω/cm2, restricted permeability to macromolecules—with apparent permeability coefficients (Papp) of 6.3 × 10−7 cm/s for 10 kDa and 2.7 × 10−7 cm/s for 70 kDa FITC–dextran—and expression of tight junctional complex (TJC) proteins such as vascular endothelial cadherin (VE-cad) and Zonula Occludens-1 (ZO-1). Furthermore, low-density lipoprotein receptor-related protein 1 (LRP1), a key receptor stably expressed in these two NVU cell types, was utilized as a critical indicator to assess the integrity of the BBB micro-organ model and its responsiveness to pathophysiological stimuli, particularly under thrombotic conditions. This study not only validates the feasibility of constructing a functionally competent BBB micro-organ model using DSMS films integrated with NVU cells but also provides a promising in vitro platform for subsequent studies on the BBB-related pathological mechanisms and the evaluation of drug permeability across the BBB.