德氏乳杆菌C-S裂解酶的研究保加利亚菌ATCC BAA-365及其在食品香精应用中的潜在作用

A. Allegrini, A. Astegno, V. La Verde, P. Dominici
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引用次数: 17

摘要

挥发性硫醇对许多饮料和食品的香气有很大的影响。因此,控制它们的形成与C-S裂解酶的酶活性有关,在涉及食品香料的工业应用中具有重要意义。在此,我们对来自德尔布鲁氏乳杆菌亚杆菌的推定的吡哆醛5'-磷酸(PLP)依赖性C-S裂解酶进行了光谱和功能表征。保加利亚的ATCC BAA-365 (LDB C-S裂解酶)。重组LDB C-S裂解酶在溶液中以四聚体形式存在,表现出以PLP为辅因子的酶的光谱特性。该酶对含硫氨基酸具有广泛的底物特异性,其中氨基乙基- l-半胱氨酸和l-胱氨酸是l-半胱氨酸和l-半胱氨酸最有效的底物。值得注意的是,该蛋白在体外也显示出半胱氨酸- s缀合β-裂解酶活性,并且能够将半胱氨酸化的底物前体裂解成相应的风味贡献硫醇,催化效率高于l -半胱氨酸。然而,与其他乳酸菌的类似酶不同,LDB C-S裂解酶不能对l -蛋氨酸产生α,γ-消除活性,从而产生甲硫醇,而甲硫醇是风味形成的重要化合物。根据我们的研究结果,可以预期乳酸杆菌C-S裂解酶的成味潜力及其在增强食品风味方面的应用的未来发展。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Characterization of C-S lyase from Lactobacillus delbrueckii subsp. bulgaricus ATCC BAA-365 and its potential role in food flavour applications
Volatile thiols have substantial impact on the aroma of many beverages and foods. Thus, the control of their formation, which has been linked to C-S lyase enzymatic activities, is of great significance in industrial applications involving food flavours. Herein, we have carried out a spectroscopic and functional characterization of a putative pyridoxal 5'-phosphate (PLP)-dependent C-S lyase from the lactic acid bacterium Lactobacillus delbrueckii subsp. bulgaricus ATCC BAA-365 (LDB C-S lyase). Recombinant LDB C-S lyase exists as a tetramer in solution and shows spectral properties of enzymes containing PLP as cofactor. The enzyme has a broad substrate specificity toward sulphur-containing amino acids with aminoethyl-L-cysteine and L-cystine being the most effective substrates over L-cysteine and L-cystathionine. Notably, the protein also reveals cysteine-S-conjugate β-lyase activity in vitro, and is able to cleave a cysteinylated substrate precursor into the corresponding flavour-contributing thiol, with a catalytic efficiency higher than L-cystathionine. Contrary to similar enzymes of other lactic acid bacteria however, LDB C-S lyase is not capable of α,γ-elimination activity towards L-methionine to produce methanethiol, which is a significant compound in flavour development. Based on our results, future developments can be expected regarding the flavour-forming potential of Lactobacillus C-S lyase and its use in enhancing food flavours.
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