Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase

Noreldeen H. Abdallah; Miriam Schlumpberger; Darragh A. Gaffney; John P. Hanrahan; Joseph M. Tobin; Edmond Magner

doi:10.1016/j.molcatb.2014.06.007

Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase

Noreldeen H. Abdallah
, Miriam Schlumpberger
, Darragh A. Gaffney
, John P. Hanrahan
, Joseph M. Tobin
, Edmond Magner

Research output: Contribution to journal › Article › peer-review

Abstract

The activity and stability of Candida antartica lipase B (CALB) and cytochrome c immobilised onto SBA-15 and a porous spherical silicate material (PPS) were examined. The materials possess similar pore diameters but have different morphologies, pore volumes and surface areas. CALB exhibited higher catalytic activity and stability on SBA-15 when compared to PPS, while cytochrome c showed similar catalytic activity on both materials. The activity of CALB immobilised on SBA-15 was retained (95%) after 7 uses, while CALB immobilised on PPS retained only 43% activity. Such changes can be mainly ascribed to the different physical properties (pore volume, surface area and pore shape) of the supports.

Original language	English
Pages (from-to)	82-88
Number of pages	7
Journal	Journal of Molecular Catalysis B: Enzymatic
Volume	108
DOIs	https://doi.org/10.1016/j.molcatb.2014.06.007
Publication status	Published - Oct 2014

Keywords

Cytochrome c
Immobilisation
Lipase
Mesoporous silicate

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10.1016/j.molcatb.2014.06.007

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title = "Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase",

abstract = "The activity and stability of Candida antartica lipase B (CALB) and cytochrome c immobilised onto SBA-15 and a porous spherical silicate material (PPS) were examined. The materials possess similar pore diameters but have different morphologies, pore volumes and surface areas. CALB exhibited higher catalytic activity and stability on SBA-15 when compared to PPS, while cytochrome c showed similar catalytic activity on both materials. The activity of CALB immobilised on SBA-15 was retained (95\%) after 7 uses, while CALB immobilised on PPS retained only 43\% activity. Such changes can be mainly ascribed to the different physical properties (pore volume, surface area and pore shape) of the supports.",

keywords = "Cytochrome c, Immobilisation, Lipase, Mesoporous silicate",

author = "Abdallah, \{Noreldeen H.\} and Miriam Schlumpberger and Gaffney, \{Darragh A.\} and Hanrahan, \{John P.\} and Tobin, \{Joseph M.\} and Edmond Magner",

year = "2014",

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doi = "10.1016/j.molcatb.2014.06.007",

language = "English",

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journal = "Journal of Molecular Catalysis B: Enzymatic",

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TY - JOUR

T1 - Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase

AU - Abdallah, Noreldeen H.

AU - Schlumpberger, Miriam

AU - Gaffney, Darragh A.

AU - Hanrahan, John P.

AU - Tobin, Joseph M.

AU - Magner, Edmond

PY - 2014/10

Y1 - 2014/10

N2 - The activity and stability of Candida antartica lipase B (CALB) and cytochrome c immobilised onto SBA-15 and a porous spherical silicate material (PPS) were examined. The materials possess similar pore diameters but have different morphologies, pore volumes and surface areas. CALB exhibited higher catalytic activity and stability on SBA-15 when compared to PPS, while cytochrome c showed similar catalytic activity on both materials. The activity of CALB immobilised on SBA-15 was retained (95%) after 7 uses, while CALB immobilised on PPS retained only 43% activity. Such changes can be mainly ascribed to the different physical properties (pore volume, surface area and pore shape) of the supports.

AB - The activity and stability of Candida antartica lipase B (CALB) and cytochrome c immobilised onto SBA-15 and a porous spherical silicate material (PPS) were examined. The materials possess similar pore diameters but have different morphologies, pore volumes and surface areas. CALB exhibited higher catalytic activity and stability on SBA-15 when compared to PPS, while cytochrome c showed similar catalytic activity on both materials. The activity of CALB immobilised on SBA-15 was retained (95%) after 7 uses, while CALB immobilised on PPS retained only 43% activity. Such changes can be mainly ascribed to the different physical properties (pore volume, surface area and pore shape) of the supports.

KW - Cytochrome c

KW - Immobilisation

KW - Lipase

KW - Mesoporous silicate

UR - https://www.scopus.com/pages/publications/84905192116

U2 - 10.1016/j.molcatb.2014.06.007

DO - 10.1016/j.molcatb.2014.06.007

M3 - Article

AN - SCOPUS:84905192116

SN - 1381-1177

VL - 108

SP - 82

EP - 88

JO - Journal of Molecular Catalysis B: Enzymatic

JF - Journal of Molecular Catalysis B: Enzymatic

ER -

Comparison of mesoporous silicate supports for the immobilisation and activity of cytochrome c and lipase

Abstract

Keywords

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