作者
Pedro Reis, Krister Holmberg, Heribert Watzke, Martin E Leser, Reinhard Miller
发表日期
2009/3/1
来源
Advances in colloid and interface science
卷号
147
页码范围
237-250
出版商
Elsevier
简介
Lipases are acyl hydrolases that play a key role in fat digestion by cleaving long-chain triglycerides into polar lipids. Due to an opposite polarity between the enzyme (hydrophilic) and their substrates (lipophilic), lipase reaction occurs at the interface between the aqueous and the oil phases. Hence, interfaces are the key spots for lipase biocatalysis and an appropriate site for modulating lipolysis. Surprisingly enough, knowledge about the effects of the interfacial composition on lipase catalysis is still limited and only described by the term “interfacial quality”. Recent systematic studies based on a biophysical approach allowed for the first time to show the effects of the interfacial microenvironment on lipase catalysis. These studies demonstrate that lipase activity as a function of interfacial composition is more attributed to substrate inaccessibility rather than to enzyme denaturation or inactivation, as it is often …
引用总数
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学术搜索中的文章
P Reis, K Holmberg, H Watzke, ME Leser, R Miller - Advances in colloid and interface science, 2009