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

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• 作者：Ying Liu^a ; Yan Yuan^a ; Xiao-yu Lei^a ; Hong Yang^a ; S.A. Ibrahim^b ; Wen Huang^a ; ^{lyly@webmail.hzau.edu.cn} ; ^{huangwen@mail.hzau.edu.cn}
• 关键词：Lentinula edodes ; ¦Ã-Glutamyl transpeptidase ; l-Cysteine sulphoxide lyase ; Purification ; Formaldehyde
• 刊名：Food Chemistry
• 出版年：2013
• 出版时间：15 June, 2013
• 年：2013
• 卷：138
• 期：4
• 页码：2174-2179
• 全文大小：384 K

文摘

In this study, ¦Ã-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 ¡ãC with an optimum activity at 37 ¡ãC. C-S lyase was stable at pH 8.0-9.0 with an optimum pH of 8.5, and was stable at 20-60 ¡ãC with an optimum activity at 40 ¡ãC. The present work supports the study of the mechanism of endogenous formaldehyde in L. edodes.