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Featured researches published by Dankui Liao.


Food Chemistry | 2014

Purification and characterization of antioxidative peptides from round scad (Decapterus maruadsi) muscle protein hydrolysate

Haiping Jiang; Tianzhe Tong; Jianhua Sun; Yuanjin Xu; Zhongxing Zhao; Dankui Liao

Muscle protein from round scad (Decapterus maruadsi) was hydrolyzed with five commercial proteases, namely, Alcalase, neutral protease, papain, pepsin, and trypsin. Round scad hydrolysate (RSH) prepared with Alcalase demonstrated high antioxidative activity. After ultrafiltration, RSH-III fraction (MW<5kDa) exhibited the strongest activity. Then, RSH-III was purified by gel filtration chromatography (Sephadex G-15) and separated into four fractions (A, B, C, and D), of which fraction B showed the highest antioxidative activity and was further purified using reverse-phase high-performance liquid chromatography twice. The purified peptides were identified as His-Asp-His-Pro-Val-Cys (706.8Da) and His-Glu-Lys-Val-Cys (614.7Da) by matrix-assisted laser desorption ionization time-of-flight/time-of-flight mass spectrometry. Subsequently, the identified peptides were synthesized, and their antioxidative activities were verified. Results indicated that the two novel peptides isolated from round scad muscle protein can be developed into antioxidative ingredients in functional foods.


Food Chemistry | 2015

Rapid purification and characterization of angiotensin converting enzyme inhibitory peptides from lizard fish protein hydrolysates with magnetic affinity separation

Xiongdiao Lan; Dankui Liao; Shanguang Wu; Feng Wang; Jianhua Sun; Zhangfa Tong

In this study, angiotensin converting enzyme (ACE) inhibitory peptides from lizard fish protein hydrolysate with neutral protease were purified through magnetic affinity separation. Magnetic agarose microsphere was prepared by reverse-phase microemulsion method, and its surface was modified with epoxy groups to immobilize ACE as a magnetic affinity medium (MAM-ACE) and then mixed with lizard fish ultrafiltration hydrolysate (<5 kDa). The MAM-ACE was recovered by a magnet. The bound peptides were released by 1M NaCl and further purified by reverse-phase high-performance liquid chromatography. The amino acid sequence of the peptide with the highest ACE inhibitory activity was identified as Gly-Met-Lys-Cys-Ala-Phe, and its IC50 was 45.7 ± 1.1 μM. The result indicates that MAM-ACE is a faster and more efficient method for purifying micro-bioactive peptides from food protein complex mixtures compared with ion exchange and gel chromatography.


Marine Drugs | 2012

Optimization of Hydrolysis Conditions for the Production of Angiotensin-I Converting Enzyme-Inhibitory Peptides and Isolation of a Novel Peptide from Lizard Fish (Saurida elongata) Muscle Protein Hydrolysate

Shanguang Wu; Jianhua Sun; Zhangfa Tong; Xiongdiao Lan; Zhongxing Zhao; Dankui Liao

Lizard fish (Saurida elongata) muscle protein was hydrolyzed using neutral protease to produce protein hydrolysate (LFPH), and the hydrolysis conditions were investigated using response-surface methodology. The optimum conditions for producing peptides with the highest angiotensin-I converting enzyme (ACE)-inhibitory activity were the following: enzyme-to-substrate ratio of 10,000 U/g, temperature of 48 °C, pH 7.0, and hydrolysis time of 2 h. Under these conditions, the ACE-inhibitory activity of LFPH and the degree of hydrolysis were 84% and 24%, respectively. A novel ACE-inhibitory peptide was isolated from LFPH using ultrafiltration, Sephadex G-15, and high-performance liquid chromatography. The amino acid sequence of the ACE-inhibitory peptide was identified as Ser-Pro-Arg-Cys-Arg (SPRCR), and its IC50 was 41 ± 1 µM.


Fluid Phase Equilibria | 1997

Excess enthalpies of (n-heptane or n-decane) + methyl tert-butyl ether + di-n-propyl ether ternary mixtures at 298.15 K

Dankui Liao; Zhangfa Tong; George C. Benson; Benjamin C.-Y. Lu

Excess molar enthalpies, measured at 298.15 K in a flow microcalorimeter, are reported for the ternary mixtures (n-heptane + methyl tert-butyl ether + di-n-propyl ether) and (n-decane + methyl tert-butyl ether + di-n-propyl ether). Smooth representations of the results are described and used to construct constant excess molar enthalpy contours on Roozeboom diagrams. It is shown that good estimates of the excess enthalpies of the ternary mixtures can be obtained from the Flory theory, using only the physical properties of the components and their binary mixtures.


Journal of Agricultural and Food Chemistry | 2018

Isolation and Characterization of Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from the Enzymatic Hydrolysate of Carapax Trionycis (the shell of the turtle Pelodiscus sinensis)

Pengying Liao; Xiongdiao Lan; Dankui Liao; Lixia Sun; Liqin Zhou; Jianhua Sun; Zhangfa Tong

Carapax Trionycis (the shell of the turtle Pelodiscus sinensis) was hydrolyzed by six different commercial proteases. The hydrolysate prepared from papain showed stronger inhibitory activity against angiotensin I-converting enzyme (ACE) than other extracts. Two noncompetitive ACE inhibitory peptides were purified successively by ultrafiltration, gel filtration chromatography, ion exchange column chromatography, and high-performance liquid chromatography (HPLC). The amino acid sequences of them were identified as KRER and LHMFK, with IC50 values of 324.1 and 75.6 μM, respectively, confirming that Carapax Trionycis is a potential source of active peptides possessing ACE inhibitory activities. Besides, both enzyme kinetics and isothermal titration calorimetry (ITC) assay showed that LHMFK could form more stable complex with ACE than KRER, which is in accordance with the better inhibitory activity of LHMFK.


Marine Drugs | 2017

Separation and Characterization of Angiotensin I Converting Enzyme (ACE) Inhibitory Peptides from Saurida elongata Proteins Hydrolysate by IMAC-Ni2+

Lixia Sun; Shanguang Wu; Liqin Zhou; Feng Wang; Xiongdiao Lan; Jianhua Sun; Zhangfa Tong; Dankui Liao

Lizard fish protein hydrolysates (LFPH) were prepared from Lizard fish (Saurida elongata) proteins possessing powerful angiotensin I converting enzyme (ACE) inhibitory activity and the fraction (LFPH-I) with high ACE inhibitory activity was obtained through ultrafiltration. The active Fraction (F2) was isolated from LFPH-I using immobilized metal affinity chromatography (IMAC-Ni2+). Analysis of amino acid levels revealed that F2 eluted from IMAC was enriched in Met, His, Tyr, Pro, Ile, and Leu compared to the crude peptide LFPH-I. F2 with the high ACE inhibitory activity (IC50 of 0.116 mg·mL−1) was further separated by a reverse-phase column to yield a novel ACE inhibitory peptide with IC50 value of 52 μM. The ACE inhibitory peptide was identified as Arg-Tyr-Arg-Pro, RYRP. The present study demonstrated that IMAC may be a useful tool for the separation of ACE inhibitory peptides from protein hydrolysate.


Journal of Materials Chemistry B | 2017

Facile synthesis of hierarchical N-doped hollow porous carbon whiskers with ultrahigh surface area via synergistic inner–outer activation for casein hydrolysate adsorption

Xin He; Pengru Liu; Jing Liu; Yaseen Muhammad; Meiping Zhu; Jianhua Sun; Xuemin Cui; Dankui Liao; Zhangfa Tong

N-doped hollow porous carbon materials have attracted significant scientific interest in the field of peptide adsorption, drug delivery and catalysis. However, their facile synthesis is still a challenge due to the lack of an ideal template and effective route for high specific surface area (SSA). In this work, we report a facile approach for preparing N-doped hollow porous carbon whiskers (HPCWs) by using CaCO3 whiskers as a green template and double inner-activating agent. Two inner activators, CO2 and Ca(OH)2, are generated from the CaCO3 whisker template during the carbonization process. Among them, Ca(OH)2 was formed by H2O vapors reacting with the remaining template CaO. Attributed to the drastic synergistic effect of inner-activation (CO2 or Ca(OH)2) and outer-activation (KOH), the synthesized HPCWs exhibit ultrahigh SSA (3007 m2 g-1), the largest pore volume (2.63 cm3 g-1) and a controllable proportion of micropores (Sm/St, 60-86%). These intriguing pore structure characteristics of HPCWs endow with them rich target-oriented applications, as exemplified by their outstanding adsorption for casein hydrolysate (10 080 mg g-1), which is two orders of magnitude (102) higher than that of common porous materials. This facile and green synthesis strategy may pave a new way to prepare hollow porous carbon materials with the desired pore structure and high surface area for numerous applications.


Pharmaceutical Biology | 2012

Rapid and simple colorimetric assay for screening angiotensin I-converting enzyme inhibitors

Shanguang Wu; Jianhua Sun; Zhangfa Tong; Xiongdiao Lan; Bing Shu; Youyan Liu; Dankui Liao

Context: Angiotensin-converting enzyme (ACE) is one of the main regulators of blood pressure through its action on the renin-angiotensin system. ACE inhibitory peptides from natural materials inhibit ACE activity and have considerable importance as antihypertensive agents. Objective: A new chromogenic reaction method for determining hippuric acid (HA) and angiotensin I-converting enzyme (ACE) inhibitor activity was developed. Materials and methods: This method is based on the reaction of HA with p-dimethylaminobenzaldehyde in the presence of quinoline, acetate, and acetic anhydride. The red–orange formation product in the reaction has a stable absorbance in the visible region and it was determined at 478 nm. The assay conditions were optimized and by using an ACE concentration of 12 mU/mL in enzymatic reaction, the method was applied to monitor the IC50 values (the concentration of inhibitor required to inhibit 50% of the ACE activity) for captopril and Saurida elongata (Synodontidae) muscle protein hydrolyzate. Results: With the proposed method, IC50 values for captopril and Saurida elongata muscle protein hydrolyzate were determined as 0.0123 µM and 0.1648 mg/mL, respectively. Those results correspond to the IC50 values of 0.0109 µM and 0.1820 mg/mL obtained by high-performance liquid chromatography (HPLC) method. Discussion and conclusion: The proposed method is rapid, accurate, reproducible and convenient, and suitable for screening ACE inhibitor peptides from food materials while it does not require HA extraction from the components of the ACE activity assay reaction.


Journal of Functional Foods | 2015

Purification and identification of Angiotensin-I Converting Enzyme (ACE) inhibitory peptide from lizard fish (Saurida elongata) hydrolysate

Shanguang Wu; Xuezhen Feng; Xiongdiao Lan; Yuanjin Xu; Dankui Liao


Chemical Communications | 2017

N-Doped porous graphitic carbon with multi-flaky shell hollow structure prepared using a green and ‘useful’ template of CaCO3 for VOC fast adsorption and small peptide enrichment

Xin He; Huaju Sun; Meiping Zhu; Muhammad Yaseen; Dankui Liao; Xuemin Cui; Haoyu Guan; Zhangfa Tong; Zhenxia Zhao

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