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| 1 | Purification and Characterization of a New Thermostable κ-CarrageenasefromtheMarineBacterium Pseudoalteromonas sp. QY203显示文摘A new extracellular κ-carrageenase, namely CgkP, 34.0 kDa in molecular weight, was purified from Pseudoalteromonas sp. QY203. CgkP showed relatively high activity at acidities ranging from pH6.0 to pH9.0 and temperatures ranging from 30℃ to 50℃ with the highest activity at 45℃ and pH7.2. Sodium chloride increased its activity markedly, and KCl increased its activity slightly. The divalent and trivalent metal ions including Cu2+ , Ni2+ , Zn2+ , Mn2+ , Al3+ and Fe3+ significantly inhibited its activity, while Mg2+ did not. CgkP remained 70% of original activity after being incubated at 40℃ for 48 h, and remained 80% of the activity after being incubated at 45℃ for 1 h. It exhibited endo-κ-carrageenase activity, mainly depolymerizing the κ-carrageenan into disaccharide and tetrasaccharide. CgkP was more thermostable than most of previously reported κ-carrageenases with a potential of being used in industry. | LI Shangyong JIA Panpan WANG Linna YU Wengong HAN Feng | 2013 | Journal of Ocean University of China2013，12，1： | 10 |
| 2 | Cloning and Characterization of a New κ-Carrageenase Gene from Marine Bacterium Pseudoalteromonas sp. QY203显示文摘κ-carrageenan oligosaccharides exhibit various biological activities. Enzymatic degradation by κ-carrageenase is safe and controllable. Therefore, κ-carrageenases have captured more and more attentions. In this study, a κ-carrageenase encoding gene, cgk X, was cloned from Pseudoalteromonas sp. QY203 with degenerate and inverse PCR. It comprised an ORF of 1194 bp in length, encoding a protein with 397 amino acid residues. Cgk X is a new member of glycoside hydrolase family 16. The deduced amino acid sequence shared a high similarity with Cgk X of Pseudoalteromonas κ-carrageenase; however, the recombinant Cgk X showed different biochemical characteristics. The recombinant enzyme was most active at p H 7.0 and 55℃ in the presence of 300 mmol L^(^(-1))Na Cl. It was stable in a broad range of acidity ranging from p H 3.0 to p H 10.0 when temperature was below 40℃. More than 80% of its activity was maintained after being incubated at p H 3.6–10.0 and 4℃ for 24 h. Cgk X retained more than 90% of activity after being incubated at 40℃ for 1 h. EDTA and SDS(1 mmol L^(-1)) did not inhibit its activity. Cgk X hydrolyzed κ-carrageenan into disaccharide and tetrasaccharide as an endo-cleaver. All these characteristics demonstrated that Cgk X is applicable to both κ-carrageenan oligosaccharide production and κ-carrageenase structure-function research. | XU Xiaoyan LI Shangyong YANG Xuemei YU Wengong HAN Feng | 2015 | Journal of Ocean University of China2015，14，6： | 5 |
| 3 | Cartilage oligomeric matrix protein is an endogenous β-arrestin-2-selective allosteric modulator of AT1 receptor counteracting vascular injury显示文摘Compelling evidence has revealed that biased activation of G protein-coupled receptor(GPCR)signaling,including angiotensin II(AngII)receptor type 1(AT1)signaling,plays pivotal roles in vascular homeostasis and injury,but whether a clinically relevant endogenous biased antagonism of AT1 signaling exists under physiological and pathophysiological conditions has not been clearly elucidated.Here,we show that an extracellular matrix protein,cartilage oligomeric matrix protein(COMP),acts as an endogenous allosteric biased modulator of the AT1 receptor and its deficiency is clinically associated with abdominal aortic aneurysm(AAA)development.COMP directly interacts with the extracellular N-terminus of the AT1 via its EGF domain and inhibits AT1-β-arrestin-2 signaling,but not Gq or Gi signaling,in a selective manner through allosteric regulation of AT1 intracellular conformational states.COMP deficiency results in activation of AT1a-β-arrestin-2 signaling and subsequent exclusive AAA formation in response to AngII infusion.AAAs in COMP–/–or ApoE–/–mice are rescued by AT1a orβ-arrestin-2 deficiency,or the application of a peptidomimetic mimicking the AT1-binding motif of COMP.Explorations of the endogenous biased antagonism of AT1 receptor or other GPCRs may reveal novel therapeutic strategies for cardiovascular diseases. | Yi Fu Yaqian Huang Zhao Yang Yufei Chen Jingang Zheng Chenfeng Mao Zhiqing Li Zhixin Liu Bing Yu Tuoyi Li Meili Wang Chanjuan Xu Yiwei Zhou Guizhen Zhao Yiting Jia Wei Guo Xin Jia Tao Zhang Li Li Ziyi Liu Shengchao Guo Mingliang Ma Heng Zhang Bo Liu Junbao Du Wengong Wang Chaoshu Tang Pei Gao Qingbo Xu Xian Wang Jianfeng Liu Jinpeng Sun Wei Kong | 2021 | Cell Research2021，31，7： | 2 |
| 4 | A New κ-Carrageenase Cgk S from Marine Bacterium Shewanella sp. Kz7显示文摘A new κ-carrageenase gene cgk S was cloned from marine bacterium Shewanella sp. Kz7 by using degenerate and site-finding PCR. The gene was comprised of an open reading frame of 1224 bp, encoding 407 amino acid residues, with a signal peptide of 24 residues. Based on the deduced amino acid sequence, the κ-carrageenase Cgk S was classified into the Glycoside Hydrolase family 16. The cgk S gene was expressed in Escherichia coli, and the recombinant enzyme was purified to homogeneity with a specific activity of 716.8 U mg-1 and a yield of 69%. Recombinant Cgk S was most active at 45℃ and p H 8.0. It was stable at p H 6.0–9.0 and below 30℃. The enzyme did not require Na Cl for activity, although its activity was enhanced by Na Cl. Cgk S degraded κ-carrageenan in an endo-fashion releasing tetrasaccharides and disaccharides as main hydrolysis products. | WANG Linna LI Shangyong ZHANG Shilong LI Jiejing YU Wengong GONG Qianhong | 2015 | Journal of Ocean University of China2015，14，4： | 2 |
| 5 | Enhancing the Thermostability of a Novel β-agarase AgaB through Directed Evolution显示文摘 | Chao Shi Xinzhi Lu Cuiping Ma Yiming Ma Xiaoyan Fu Wengong Yu | 2008 | Applied Biochemistry and Biotechnology2008，，1： | 1 |
| 6 | Purification and Refolding of a Novel β-Agarase from Inclusion Body of E. coli显示文摘β-agarase AgaB appears to represent a new family of glycoside hydrolase; it is structurally and functionally different from other known agarases. In the present study, AgaB was expressed with a temperature-inducible expression system in E. coli BL21 (DE3) as a fusion protein bearing a C-terminal hexahistidine tag. The protein existed mainly in the form of inclusion body. After being washed and solubilized, AgaB in inclusion body was denatured and purified to electrophoretic purity by immobilized metal affinity chromatography. The purified AgaB was then refolded using a simple pulse dilution method, and the refolded AgaB showed a high specific hydrolysis activity of about 1600 units /mg protein. Forty milligrams of refolded pure protein were obtained from 1L of culture. | ZHANG Li, LU Xinzhi, HAN Feng, MA Cuiping, and YU Wengong* Marine Drug and Food Institute, Ocean University of China, Qingdao 266003, P.R. China | 2007 | Journal of Ocean University of China2007，6，1： | 1 |
| 7 | Increasing the transient expression of GUS gene in Porphyra yezoensis by 18S rDNA targeted homologous recombination显示文摘 | Hongquan Liu Wengong Yu Jixun Dai Qianhong Gong Kunfeng Yang Yaping Zhang | 2003 | Journal of Applied Phycology2003，，5： | 1 |
| 8 | The hydrophobic cluster on the surface of protein is the key structural basis for the SDS-resistance of chondroitinase VhChlABC显示文摘The application of chondroitinase requires consideration of the complex microenvironment of the target.Our previous research reported a marine-derived sodium dodecyl sulfate(SDS)-resistant chondroitinase VhChlABC.This study further investigated the mechanism of VhChlABC resistance to SDS.Focusing on the hydrophobic cluster on its strong hydrophilic surface,it was found that the reduction of hydrophobicity of surface residues Ala181,Met182,Met183,Ala184,Val185,and Ile305 significantly reduced the SDS resistance and stability.Molecular dynamics(MD)simulation and molecular docking analysis showed that I305G had more conformational flexibility around residue 305 than wild type(WT),which was more conducive to SDS insertion and binding.The affinity of A181G,M182A,M183A,V185A and I305G to SDS was significantly higher than that of WT.In conclusion,the surface hydrophobic microenvironment composed of six residues was the structural basis for SDS resistance.This feature could prevent the binding of SDS and the destruction of hydrophobic packaging by increasing the rigid conformation of protein and reducing the binding force of SDS-protein.The study provides a new idea for the rational design of SDS-resistant proteins and may further promote chondroitinase research in the targeted therapy of lung diseases under the pressure of pulmonary surfactant. | Juanjuan Su Hao Wu Chengying Yin Fengchao Zhang Feng Han Wengong Yu | 2024 | Marine Life Science & Technology2024，6，1： | 0 |
| 9 | Prevention of Reservoir Water Bloom by Bio-manipulation显示文摘Siminghu Reservoir already transformed into ' the algae muddy' type,and had nonclassical bio-manipulation practice using Hypophthalmichthys molitix and Aristichthys nobilis to feed the plankton,control water bloom and transform the organic matters into fish product. Through the analysis of the limited data,we think that water bloom of Siminghu Reservoir can be prevented to some extent by breeding H. molitix and A. nobilis,and it can slow down eutrophication of reservoir but cannot control the eutrophication tendency. We must take a variety of comprehensive management measures to control eutrophication from the angle of basin control,and guarantee safety of drinking water resources. | Yu Wengong | 2015 | Meteorological and Environmental Research2015，6，2： | 0 |
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