Production of protocatechualdehyde using tyrosinase purified from potato
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, Kyoung-Ja | - |
dc.contributor.author | Yang, Yong-Joon | - |
dc.date.accessioned | 2021-08-12T02:47:35Z | - |
dc.date.available | 2021-08-12T02:47:35Z | - |
dc.date.issued | 2012-08 | - |
dc.identifier.issn | 2211-3452 | - |
dc.identifier.issn | 2211-3460 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/sch/handle/2021.sw.sch/14988 | - |
dc.description.abstract | Tyrosinase is responsible for the enzymatic browning of fruits and vegetables and usually catalyze the conversion of monophenols to o-diphenols and oxidation of diphenols to corresponding quinines. However, when 3,4-dihydroxymandelic acid is provided as the substrate, it catalyzes the oxidative decarboxylation reaction to generate 3,4-dihydroxybenzaldehyde (protocatechualdehyde, PA. In the present study, tyrosinase was purified from potato with 27.9 purification fold by salting out with ammonium sulfate, DEAE-Sepharose and Sephadex G-150 column chromatography. The purified tyrosinase was confirmed by tyrosinase active staining following SDS-PAGE. Tyrosinase activity was visualized in the gel as a dark band. The molecular weight of tyrosinase from potato was 38kDa as determined by SDS-PAGE. Purified tyrosinase mediated oxidative decarboxylation of 3,4-dihydroxymandelate. The identity of the reaction product, PA was confirmed by high-performance liquid chromatography (HPLC) as well as ultraviolet spectral studies. Phenol oxidase inhibitors such as potassium cyanide, sodium azide, and phenylthiourea inhibited the participation of the active site copper of the enzyme in the catalysis. | - |
dc.format.extent | 5 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | 한국원예학회 | - |
dc.title | Production of protocatechualdehyde using tyrosinase purified from potato | - |
dc.type | Article | - |
dc.publisher.location | 대한민국 | - |
dc.identifier.doi | 10.1007/s13580-012-0098-z | - |
dc.identifier.scopusid | 2-s2.0-84866054837 | - |
dc.identifier.wosid | 000308546400004 | - |
dc.identifier.bibliographicCitation | Horticulture, Environment, and Biotechnology, v.53, no.4, pp 283 - 287 | - |
dc.citation.title | Horticulture, Environment, and Biotechnology | - |
dc.citation.volume | 53 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 283 | - |
dc.citation.endPage | 287 | - |
dc.type.docType | Article | - |
dc.identifier.kciid | ART001690682 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.description.journalRegisteredClass | kci | - |
dc.relation.journalResearchArea | Agriculture | - |
dc.relation.journalWebOfScienceCategory | Horticulture | - |
dc.subject.keywordPlus | MUSHROOM TYROSINASE | - |
dc.subject.keywordPlus | NEUROSPORA-CRASSA | - |
dc.subject.keywordPlus | IN-VITRO | - |
dc.subject.keywordPlus | ANTIOXIDANT | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | SUBSTRATE | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordAuthor | enzymatic browning | - |
dc.subject.keywordAuthor | oxidative decarboxylation | - |
dc.subject.keywordAuthor | phenol oxidase | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(31538) 22, Soonchunhyang-ro, Asan-si, Chungcheongnam-do, Republic of Korea+82-41-530-1114
COPYRIGHT 2021 by SOONCHUNHYANG UNIVERSITY ALL RIGHTS RESERVED.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.