Purification and characterisation of two enzymes related to endogenous formaldehyde in Lentinula edodes

Ying Liu; Yan Yuan; Xiao-Yu Lei; Hong Yang; SA Ibrahim; Wen Huang

doi:10.1016/j.foodchem.2012.12.038

Purification and characterisation of two enzymes related to endogenous formaldehyde in Lentinula edodes

Ying Liu
, Yan Yuan
, Xiao-Yu Lei
, Hong Yang
, SA Ibrahim
, Wen Huang

Huazhong Agricultural University

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

40 Scopus citations

Abstract

In this study, γ-glutamyl transpeptidase (GGT) and l-cysteine sulphoxide lyase (C-S lyase) were purified from the fruiting body of Lentinula edodes in three steps and then characterised. We found that GGT together with C-S lyase caused the generation of endogenous formaldehyde in L. edodes. GGT was composed of a large subunit of 41 kDa and a small subunit of 25 kDa, and C-S lyase was composed of two identical subunits of 46 kDa, as determined by SDS-PAGE. GGT was stable at pH 8.0-10.0 with an optimum pH of 8.8, and was stable at 20-50 °C with an optimum activity at 37 °C. C-S lyase was stable at pH 8.0-9.0 with an optimum pH of 8.5, and was stable at 20-60 °C with an optimum activity at 40 °C. The present work supports the study of the mechanism of endogenous formaldehyde in L. edodes. © 2012 Elsevier Ltd. All rights reserved.

Original language	English
Pages (from-to)	2174-2179
Number of pages	6
Journal	Food Chemistry
Volume	138
Issue number	4
DOIs	https://doi.org/10.1016/j.foodchem.2012.12.038
State	Published - Jun 15 2013

Keywords

γ-Glutamyl transpeptidase
Formaldehyde
l-Cysteine sulphoxide lyase
Lentinula edodes
Purification

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10.1016/j.foodchem.2012.12.038

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title = "Purification and characterisation of two enzymes related to endogenous formaldehyde in Lentinula edodes",

abstract = "In this study, γ-glutamyl transpeptidase (GGT) and l-cysteine sulphoxide lyase (C-S lyase) were purified from the fruiting body of Lentinula edodes in three steps and then characterised. We found that GGT together with C-S lyase caused the generation of endogenous formaldehyde in L. edodes. GGT was composed of a large subunit of 41 kDa and a small subunit of 25 kDa, and C-S lyase was composed of two identical subunits of 46 kDa, as determined by SDS-PAGE. GGT was stable at pH 8.0-10.0 with an optimum pH of 8.8, and was stable at 20-50 °C with an optimum activity at 37 °C. C-S lyase was stable at pH 8.0-9.0 with an optimum pH of 8.5, and was stable at 20-60 °C with an optimum activity at 40 °C. The present work supports the study of the mechanism of endogenous formaldehyde in L. edodes. {\textcopyright} 2012 Elsevier Ltd. All rights reserved.",

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author = "Ying Liu and Yan Yuan and Xiao-Yu Lei and Hong Yang and SA Ibrahim and Wen Huang",

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doi = "10.1016/j.foodchem.2012.12.038",

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AU - Liu, Ying

AU - Yuan, Yan

AU - Lei, Xiao-Yu

AU - Yang, Hong

AU - Ibrahim, SA

AU - Huang, Wen

PY - 2013/6/15

Y1 - 2013/6/15

N2 - In this study, γ-glutamyl transpeptidase (GGT) and l-cysteine sulphoxide lyase (C-S lyase) were purified from the fruiting body of Lentinula edodes in three steps and then characterised. We found that GGT together with C-S lyase caused the generation of endogenous formaldehyde in L. edodes. GGT was composed of a large subunit of 41 kDa and a small subunit of 25 kDa, and C-S lyase was composed of two identical subunits of 46 kDa, as determined by SDS-PAGE. GGT was stable at pH 8.0-10.0 with an optimum pH of 8.8, and was stable at 20-50 °C with an optimum activity at 37 °C. C-S lyase was stable at pH 8.0-9.0 with an optimum pH of 8.5, and was stable at 20-60 °C with an optimum activity at 40 °C. The present work supports the study of the mechanism of endogenous formaldehyde in L. edodes. © 2012 Elsevier Ltd. All rights reserved.

AB - In this study, γ-glutamyl transpeptidase (GGT) and l-cysteine sulphoxide lyase (C-S lyase) were purified from the fruiting body of Lentinula edodes in three steps and then characterised. We found that GGT together with C-S lyase caused the generation of endogenous formaldehyde in L. edodes. GGT was composed of a large subunit of 41 kDa and a small subunit of 25 kDa, and C-S lyase was composed of two identical subunits of 46 kDa, as determined by SDS-PAGE. GGT was stable at pH 8.0-10.0 with an optimum pH of 8.8, and was stable at 20-50 °C with an optimum activity at 37 °C. C-S lyase was stable at pH 8.0-9.0 with an optimum pH of 8.5, and was stable at 20-60 °C with an optimum activity at 40 °C. The present work supports the study of the mechanism of endogenous formaldehyde in L. edodes. © 2012 Elsevier Ltd. All rights reserved.

KW - γ-Glutamyl transpeptidase

KW - Formaldehyde

KW - l-Cysteine sulphoxide lyase

KW - Lentinula edodes

KW - Purification

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Purification and characterisation of two enzymes related to endogenous formaldehyde in Lentinula edodes

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Keywords

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