FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W45345834> ?p ?o ?g. }

• W45345834 endingPage "1887" @default.
• W45345834 startingPage "1885" @default.
• W45345834 abstract "Biocatalyst is a strong tool for preparation of enantiopure compounds through kinetic resolution or direct synthesis. However, enzymes do not always satisfy the needs of researchers for this purpose because they often do not have enough activity or selectivity toward unnatural substrates. To solve the problems, it is important to find new enzymes from nature, although researchers have tried to change enzyme activity or selectivity by mutagenesis such as random mutagenesis and rational design. Researchers have isolated a variety of enzymes from various sources such as bacteria, fungi, mammals, and plants. Diabetic enzymes such as lipases and proteases from bacteria and mammals are well characterized and utilized successfully in academic and industrial areas. The enzymes involved in mechanisms for protecting plants from insect or fungal attack are also useful in organic synthesis. Such enzymes generally catalyze reactions to produce toxic chemicals in the last step of secondary metabolism to kill predators. As an example, hydroxynitrilases from cyanogenic plants catalyze the biodegradation of cyanogenic glycosides to release hydrogen cyanide. The reverse reaction is interesting in organic synthesis because hydroxynitrilases catalyze formation of enantiopure cyanohydrins from aldehydes or ketones and hydrogen cyanide. Searching enzymes involved in the secondary metabolism of plants may provide useful biocatalysts in organic synthesis because the enzymes have a key role for synthesis of many biologically active compounds. Ginkgo biloba leaves have high anti-insect activity and biological activity. Thus, they might contain an interesting enzyme involved in the secondary metabolism and the enzyme can be useful for organic synthesis. We have chosen Ginkgo biloba leaves for finding a new enzyme because Ginkgo biloba leaves potentially contain enzymes involved in the secondary metabolism and also the study of the enzymatic activity of extracts from Ginkgo leaves has not been focused while the chemicals in them have been well characterized. Herein, we represent an enzyme activity in Ginkgo biloba leaves. Most enzymes are classified into six groups, such as oxidoreductase, transferases, hydrolases, lyases, isomerases, and ligases. Activities for oxidoreductase, hydrolase, and lyase were chosen for screening enzyme activities in Ginkgo biloba leaves because these enzymes are important in organic synthesis. We assayed the activities of peroxidase for oxidoreductase, β-amylase, nitrilase, and esterase for hydrolase, and hydroxynitrilase for lyase. Ginkgo biloba leaves were ground by a homogenizer and washed with ethyl acetate to remove organic components. Ginkgo powders were extracted with the reaction buffers for activity screening. Under the assay condition tested, Ginkgo extracts showed only the peroxidase activity (Table 1). In the assay condition, peroxidases oxidize pyrogallol to purpurogallin using hydrogenperoxide (eq. 1). The absorbance change can be monitored at 420 nm. The reaction coordinate showed clear difference between the reaction by Ginkgo extracts and the blank reaction (Figure 1)." @default.
• W45345834 created "2016-06-24" @default.
• W45345834 creator A5025263635 @default.
• W45345834 date "2006-11-20" @default.
• W45345834 modified "2023-10-14" @default.
• W45345834 title "Study of an Enzyme Activity in Extracts of Ginkgo biloba Leaves" @default.
• W45345834 cites W1970712220 @default.
• W45345834 cites W1974772724 @default.
• W45345834 cites W1985252740 @default.
• W45345834 cites W1991524668 @default.
• W45345834 cites W2015387522 @default.
• W45345834 cites W2112169196 @default.
• W45345834 cites W2112621650 @default.
• W45345834 cites W2124043771 @default.
• W45345834 cites W2133569167 @default.
• W45345834 cites W2138595670 @default.
• W45345834 cites W2145830415 @default.
• W45345834 cites W2150371887 @default.
• W45345834 cites W2157334869 @default.
• W45345834 cites W2414195091 @default.
• W45345834 doi "https://doi.org/10.5012/bkcs.2006.27.11.1885" @default.
• W45345834 hasPublicationYear "2006" @default.
• W45345834 type Work @default.
• W45345834 sameAs 45345834 @default.
• W45345834 citedByCount "3" @default.
• W45345834 countsByYear W453458342012 @default.
• W45345834 countsByYear W453458342021 @default.
• W45345834 crossrefType "journal-article" @default.
• W45345834 hasAuthorship W45345834A5025263635 @default.
• W45345834 hasBestOaLocation W453458341 @default.
• W45345834 hasConcept C181199279 @default.
• W45345834 hasConcept C185592680 @default.
• W45345834 hasConcept C2778998842 @default.
• W45345834 hasConcept C2779706397 @default.
• W45345834 hasConcept C55493867 @default.
• W45345834 hasConcept C556039675 @default.
• W45345834 hasConcept C59822182 @default.
• W45345834 hasConcept C71924100 @default.
• W45345834 hasConcept C86803240 @default.
• W45345834 hasConceptScore W45345834C181199279 @default.
• W45345834 hasConceptScore W45345834C185592680 @default.
• W45345834 hasConceptScore W45345834C2778998842 @default.
• W45345834 hasConceptScore W45345834C2779706397 @default.
• W45345834 hasConceptScore W45345834C55493867 @default.
• W45345834 hasConceptScore W45345834C556039675 @default.
• W45345834 hasConceptScore W45345834C59822182 @default.
• W45345834 hasConceptScore W45345834C71924100 @default.
• W45345834 hasConceptScore W45345834C86803240 @default.
• W45345834 hasIssue "11" @default.
• W45345834 hasLocation W453458341 @default.
• W45345834 hasOpenAccess W45345834 @default.
• W45345834 hasPrimaryLocation W453458341 @default.
• W45345834 hasRelatedWork W1934208790 @default.
• W45345834 hasRelatedWork W1973039607 @default.
• W45345834 hasRelatedWork W1973326136 @default.
• W45345834 hasRelatedWork W2083017908 @default.
• W45345834 hasRelatedWork W2099420720 @default.
• W45345834 hasRelatedWork W2248396708 @default.
• W45345834 hasRelatedWork W2373893315 @default.
• W45345834 hasRelatedWork W2396328892 @default.
• W45345834 hasRelatedWork W2894331390 @default.
• W45345834 hasRelatedWork W3128960999 @default.
• W45345834 hasVolume "27" @default.
• W45345834 isParatext "false" @default.
• W45345834 isRetracted "false" @default.
• W45345834 magId "45345834" @default.
• W45345834 workType "article" @default.