Oxidation chemistry using enzymes is approaching maturity and practical applicability in organic synthesis. Oxidoreductases (enzymes catalysing redox reactions) enable chemists to perform highly selective and efficient transformations ranging from simple alcohol oxidations to stereoselective halogenations of non‐activated C−H bonds. For many of these reactions, no “classical” chemical counterpart is known. Hence oxidoreductases open up shorter synthesis routes based on a more direct access to the target products. The generally very mild reaction conditions may also reduce the environmental impact of biocatalytic reactions compared to classical counterparts. In this Review, we critically summarise the most important recent developments in the field of biocatalytic oxidation chemistry and identify the most pressing bottlenecks as well as promising solutions.

Lipases are important industrial enzymes. Most of the lipases operate at lipid-water interfaces enabled by a mobile lid domain located over the active site. Lid protects the active site and hence responsible for catalytic activity. In pure aqueous media the lid is predominantly closed, whereas in the presence of a hydrophobic layer it is partially opened. Hence, the lid controls the enzyme activity. In the present review, we have classified lipases into different groups based on the structure of lid domains. It has been observed that thermostable lipases contain larger lid domains with two or more helices, whereas mesophilic lipases tend to have smaller lids in the form of a loop or a helix. Recent developments in lipase engineering addressing the lid regions are critically reviewed here. After on the dramatic changes in substrate selectivity, activity and thermostability have been reported. Furthermore, improved computational models now can rationalize these observations by relating it to the mobility of the lid domain. In this contribution, we summarized and critically evaluated the most recent developments in experimental and computational research on lipase lids.

Recent studies revealed the role of lipase in the pathogenicity of Malassezia restricta in dandruff and seborrheic dermatitis (D/SD). The lipase from M. restricta (Mrlip1) is considered a potential target for dandruff therapy. In this work, we performed structure-based virtual screening in Zinc database to find the natural bioactive inhibitors of Mrlip1. We identified three compounds bearing superior affinity and specificity from the Traditional Chinese Medicine database (~60,000 compounds), and their binding patterns with Mrlip1 were analyzed in detail. Additionally, we performed three sets of 100 ns MD simulations of each complex in order to understand the interaction mechanism of Mrlip1 with known inhibitor RHC80267 and the newly identified compounds such as ZINC85530919, ZINC95914464 and ZINC85530320, respectively. These compounds bind to the active site cavity and cause conformational changes in Mrlip1. The Molecular Mechanics Poisson-Boltzmann Surface Area (MMPBSA) studies suggested that the average binding energy was stronger in the case of Mrlip1-ZINC85530919 and Mrlip1-ZINC95914464. The selected natural inhibitors might act as promising lead drugs against Mrlip1. Further, the present study will contribute to various steps involved in developing and creating potent drugs for several skin diseases including dandruff.

Enzyme gewinnen immer mehr Bedeutung als Katalysatoren für organische Oxidationsreaktionen. Mit Oxidoreduktasen stehen dem Chemiker vielseitige Werkzeuge für selektive und effiziente Oxidationsreaktionen zur Verfügung. Ihr Spektrum reicht von einfachen Alkoholoxidationen bis hin zur stereoselektiven Halogenierung nicht‐aktivierter C‐H‐Bindungen. Für viele biokatalytische Oxidationen ist bisher kein chemisches Pendant bekannt. Daher ermöglichen Oxidoreduktasen kürzere Syntheserouten. Darüber hinaus sind die generell milderen Reaktionsbedingungen biokatalytischer Oxidationen attraktiv. In diesem Aufsatz fassen wir einige aktuelle Entwicklungen im Bereich der biokatalytischen Oxidation zusammen. Wir beschreiben auch derzeitige Grenzen und vielversprechende Lösungsansätze.