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Studies on the catalytic behavior of a membrane-bound lipolytic enzyme from the microalgae Nannochloropsis oceanica CCMP1779

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바이오화학분류
    • 바이오플라스틱
      1. 플라스틱
    • 바이오정밀화학
      1. 용매
      2. 화학제품
      3. 연료
    • 화장품용 기능성소재
      1. 계면활성제⁄증점제
    • 의료용 화학소재
      1. 식품첨가제
논문

Studies on the catalytic behavior of a membrane-bound lipolytic enzyme from the microalgae Nannochloropsis oceanica CCMP1779

학술지

Enzyme and microbial technology

저자명

Savvidou, Maria G.; Katsabea, Alexandra; Kotidis, Pavlos; Mamma, Diomi; Lymperopoulou, Theopisti V.; Kekos, Dimitris; Kolisis, Fragiskos N.

초록

<P><B>Abstract</B></P> <P>The catalytic behavior of a membrane-bound lipolytic enzyme (MBL-Enzyme) from the microalgae <I>Nannochloropsis oceanica</I> CCMP1779 was investigated. The biocatalyst showed maximum activity at 50 &deg;C and pH 7.0, and was stable at pH 7.0 and temperatures from 40 to 60 &deg;C. Half-lives at 60 &deg;C, 70 &deg;C and 80 &deg;C were found 866.38, 150.67 and 85.57 min respectively. Thermal deactivation energy was 68.87 kJ mol<SUP>&minus;1</SUP>. The enzyme&rsquo;s enthalpy (&Delta;<I>&Eta;</I>*), entropy (&Delta;<I>S</I>*) and Gibb&rsquo;s free energy (&Delta;<I>G</I>*) were in the range of 65.86&ndash;66.27 kJ mol<SUP>&minus;1</SUP>, 132.38&ndash;140.64 J mol<SUP> <SUP>&minus;1</SUP> </SUP> K<SUP>&minus;1</SUP> and 107.80&ndash;115.81 kJ mol<SUP>&minus;1</SUP>, respectively. Among <I>p</I>-nitrophenyl esters of fatty acids tested, MBL-Enzyme exhibited the highest hydrolytic activity against <I>p</I>-nitrophenyl palmitate (<I>p</I>NPP). The K<SUB>m</SUB> and V<SUB>max</SUB> values were found 0.051 mM and of 0.054 mmole <I>p</I>NP mg protein<SUP>&minus;1</SUP> min<SUP>&minus;1</SUP>, respectively with <I>p</I>NPP as substrate. The presence of Mn<SUP>2+</SUP> increased lipolytic activity by 68.25%, while Fe<SUP>3+</SUP> and Cu<SUP>2+</SUP> ions had the strongest inhibitory effect. MBL-Enzyme was stable in the presence of water miscible (66% of the initial activity in ethanol) and water immiscible (71% of the initial activity in <I>n</I>-octane) solvents. Myristic acid was found to be the most efficient acyl donor in esterification reactions with ethanol. Methanol was the best acyl acceptor among the primary alcohols tested.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Membane-bound lipolytic enzyme (MBL-Enzyme) from microalgae <I>Nannochloropsis oceanica</I>. </LI> <LI> Maximum hydrolytic activity at 50 &deg;C and pH 7.0; stable at pH 7.0 and up to 70 &deg;C. </LI> <LI> Highest hydrolytic activity against <I>p</I>-nitrophenyl palmitate. </LI> <LI> Stable in the presence of water miscible and water immiscible solvents. </LI> <LI> Myristic acid is the most efficient acyl donor in esterification reactions. </LI> </UL> </P> <P><B>Graphical abstract</B></P> <P>[DISPLAY OMISSION]</P>

발행연도

2018

발행기관

Elsevier

ISSN

0141-0229

ISSN

1879-0909

116

페이지

pp.64-71

주제어

Membrane-bound lipolytic enzyme (MBL-Enzyme); Nannochloropsis oceanica CCMP1779; Biochemical properties; Hydrolytic activity; Esterification activity

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1 2023-12-11
2 2023-12-11

논문; 2018-09-01

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