Enzymatic Properties of an Extracellular Phospholipase C Purified from a Marine Streptomycete

Mo, SangJoon; Kim, Jae Heon; Cho, Ki Woong

doi:10.1271/bbb.90323

Cited by 20 publications

(3 citation statements)

References 6 publications

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“…Phospholipase C (PLC) enzyme cleaves phospholipid near the phosphate group thus producing phosphocholine and diacylglycerol. PCL enzymes play an important role in signal transduction pathways (Bunney and Katan 2011;BamjiMirza and Yao 2015;Mo et al 2009;Fisher and Mehendra 2009;Worthington Enzyme Manual).…”

Section: Introductionmentioning

confidence: 99%

Zeta potential and surface charge of DPPC and DOPC liposomes in the presence of PLC enzyme

2016

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Zeta potential of liposomes is often measured in studies of their properties and/or applications. However, there are not many papers published in which zeta potential was determined during enzymatic reaction of a lipid. Therefore in this paper size, polydispersity index, and zeta potentials of 1,2-dipalmitoylsn-glycero-3-phosphatidylcholine (DPPC) and 1,2-dioleoyl-sn-glycero-3-phosphatidylcholine (DOPC) liposomes were investigated in 1 mM NaCl (pH 6.2) and phosphate buffer (pH 8.1) during 60 min of phospholipase C action at 20 and 37°C. The hydrocarbon chains saturation differ these two phospholipids what appears in some differences in the zeta potential changes during the hydrolysis reaction run. The polydispersity index of the liposomes indicates that they are relatively stable and monodisperse, except for DPPC in phosphate buffer where up to 30 % of the initial amount forms larger size moieties, possibly aggregates of the liposomes, enzyme and the hydrolysis products. However, in this buffer zeta potential of the liposomes practically does not change during PLC action. Also the changes of zeta potential of DOPC liposomes are minor, although their negative values are much smaller than those of DPPC at both temperatures. These small changes of the potential may be due to compression of the diffuse double layer by present phosphate buffer. However, distinct changes of the zeta potentials in the presence of PLC take place in NaCl solution. The observed changes can be explained by reorientation of the phospholipid polar heads and their different density on DPPC and DOPC surface of the liposomes. Although it appeared that the zeta potential is not a very sensitive parameter for tracking the hydrolysis reaction in phosphate buffer, generally zeta potential enables the characterization of such reactions through determination of electrokinetic properties of liposomes as well as the polydispersity and size distribution of the liposomes do.

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Section: Introductionmentioning

confidence: 99%

Zeta potential and surface charge of DPPC and DOPC liposomes in the presence of PLC enzyme

2016

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“…Some lipases could actively hydrolyze different oils, indicating that they may have potential applications in industry [34]. In 2009, a novel extracellular phospholipase C was purified from a marine streptomycete , which was selected from approximately 400 marine bacteria by Mo et al Its enzyme activity was optimal at pH 8.0 at 45 ºC, and it hydrolyzed only phosphatidylcholine[35]. …”

Section: Lipasementioning

confidence: 99%

Research and Application of Marine Microbial Enzymes: Status and Prospects

2010

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Over billions of years, the ocean has been regarded as the origin of life on Earth. The ocean includes the largest range of habitats, hosting the most life-forms. Competition amongst microorganisms for space and nutrients in the marine environment is a powerful selective force, which has led to evolution. The evolution prompted the marine microorganisms to generate multifarious enzyme systems to adapt to the complicated marine environments. Therefore, marine microbial enzymes can offer novel biocatalysts with extraordinary properties. This review deals with the research and development work investigating the occurrence and bioprocessing of marine microbial enzymes.

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“…At present, phospholipases from microorganisms have been attracting more attention due to the advantage that their production could be mass prepared via fermentation. Currently, the microorganisms that have been reported with the capability to secrete phospholipases include Candida albicans [ 5 ], Lactobacillus casei [ 6 ], Serratia marcescens [ 7 ], Saccharomyces cerevisiae [ 8 , 9 ], and Streptomyces [ 10 ]. PLA 1 (EC 3.1.1.32) has been verified to show specific hydrolyzing ability against the sn-1 acyl group of phospholipids with the production of lysophosphatidylcholine and a single fatty acid.…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Phospholipase A1 Using a Protein-Inorganic Hybrid System

et al. 2021

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In this study, four kinds of phospholipase A1-metal (Al/Co/Cu/Mn) hybrid nanostructures were prepared for enhancing the stability of the free PLA1. The formed hybrid complexes were characterized by scanning electron microscope (SEM), Fourier infrared spectroscopy (FTIR), and X-ray diffraction (XRD). The stability and substrate specificity of immobilized enzymes were subsequently determined. After immobilization, the temperature tolerance of PLA1–metal hybrid nanostructures was enhanced. The relative activity of PLA1–Al/Co/Cu hybrid nanostructures remained above 60% at 50 °C, while that of free enzyme was below 5%. The thermal transition temperature measured by differential scanning calorimetry (DSC) was found to increase from 65.59 °C (free enzyme) to 173.14 °C, 123.67 °C, 96.31 °C, and 114.79 °C, referring to PLA1–Cu/Co/Al/Mn hybrid nanostructures, respectively. Additionally, after a storage for fourteen days at 4 °C, the immobilized enzymes could exhibit approximately 60% of the initial activity, while the free PLA1 was inactivated after four days of storage. In brief, using Co2+, Cu2+, Al3+, and Mn2+ as the hybridization materials for immobilization could improve the catalytic properties and stability of the free PLA1, suggesting a promising method for a wider application of PLA1 in many fields such as food, cosmetics, and the pharmaceutical industry.

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Enzymatic Properties of an Extracellular Phospholipase C Purified from a Marine Streptomycete

Cited by 20 publications

References 6 publications

Zeta potential and surface charge of DPPC and DOPC liposomes in the presence of PLC enzyme

Zeta potential and surface charge of DPPC and DOPC liposomes in the presence of PLC enzyme

Research and Application of Marine Microbial Enzymes: Status and Prospects

Immobilization of Phospholipase A1 Using a Protein-Inorganic Hybrid System

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