Characterization of blueberry (Vaccinium corymbosum L.) catechol oxidases III binding mechanism in response to selected substrates and inhibitors. (15th March 2022)
- Record Type:
- Journal Article
- Title:
- Characterization of blueberry (Vaccinium corymbosum L.) catechol oxidases III binding mechanism in response to selected substrates and inhibitors. (15th March 2022)
- Main Title:
- Characterization of blueberry (Vaccinium corymbosum L.) catechol oxidases III binding mechanism in response to selected substrates and inhibitors
- Authors:
- Wei, Yulong
Yu, Ning
Zhu, Yue
Jia, Chengli
Xiao, Yuhang
Zhao, Yue
Cai, Pengju
Zhao, Wanbin
Ju, Mengmeng
Wu, Tongtong
Gan, Zhilin
Sun, Aidong - Abstract:
- Abstract: Catechol oxidase (CO) is one of the enzymes that cause browning of blueberries and related products. In-depth study of its properties will help reduce the loss caused by it. The optimal pH for catechol (CAT), 3, 4-dihydroxyphenylacetic acid (DOPAC), 4-methylcatechol (4-MeCAT), 3-hydroxytyramine hydrochloride (3-HTH), and pyrogallol (PG) substrates were 6.0, 4.0, 3.0, 6.5, and 4.5, respectively. The substrates with catechol structure selected in the experiment can react with CO, except protocatechuic acid (PCA). Caffeic acid (CA) may be the most suitable natural substrate for this blueberry CO. The K + and Na + have little effect on the CO activity. Li +, Mg 2+, Cu 2+, Zn 2+, and Ca 2+ could increase enzyme activity at low concentrations (0–5 mmol/L). The most effective inhibitor in the experiment was tropolone (TPL; IC 50 = 10.01 ± 0.11 μmol/L), followed by 1, 4-benzoquinone (1, 4-BQ; IC 50 = 34.84 ± 0.56 μmol/L). It was found that the carboxyl or phenolic hydroxyl groups in the substrates and inhibitors played an important role in binding to the catalytic cavity. The position of THR320 (HB1 + 1) was a key in regulating enzyme activity. The sugars should be in high concentration condition to inhibit enzyme activity. Highlights: Specificity of substrate catalysis and binding for blueberry CO Ⅲ was characterized. Effect and mechanism of different inhibitors on CO Ⅲ inhibition were demonstrated. The type and location of functional groups can affect the inhibitor'sAbstract: Catechol oxidase (CO) is one of the enzymes that cause browning of blueberries and related products. In-depth study of its properties will help reduce the loss caused by it. The optimal pH for catechol (CAT), 3, 4-dihydroxyphenylacetic acid (DOPAC), 4-methylcatechol (4-MeCAT), 3-hydroxytyramine hydrochloride (3-HTH), and pyrogallol (PG) substrates were 6.0, 4.0, 3.0, 6.5, and 4.5, respectively. The substrates with catechol structure selected in the experiment can react with CO, except protocatechuic acid (PCA). Caffeic acid (CA) may be the most suitable natural substrate for this blueberry CO. The K + and Na + have little effect on the CO activity. Li +, Mg 2+, Cu 2+, Zn 2+, and Ca 2+ could increase enzyme activity at low concentrations (0–5 mmol/L). The most effective inhibitor in the experiment was tropolone (TPL; IC 50 = 10.01 ± 0.11 μmol/L), followed by 1, 4-benzoquinone (1, 4-BQ; IC 50 = 34.84 ± 0.56 μmol/L). It was found that the carboxyl or phenolic hydroxyl groups in the substrates and inhibitors played an important role in binding to the catalytic cavity. The position of THR320 (HB1 + 1) was a key in regulating enzyme activity. The sugars should be in high concentration condition to inhibit enzyme activity. Highlights: Specificity of substrate catalysis and binding for blueberry CO Ⅲ was characterized. Effect and mechanism of different inhibitors on CO Ⅲ inhibition were demonstrated. The type and location of functional groups can affect the inhibitor's activity. The inhibitory effects of different sugars on CO Ⅲ were explored. … (more)
- Is Part Of:
- Lebensmittel-Wissenschaft + Technologie =. Volume 158(2022)
- Journal:
- Lebensmittel-Wissenschaft + Technologie =
- Issue:
- Volume 158(2022)
- Issue Display:
- Volume 158, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 158
- Issue:
- 2022
- Issue Sort Value:
- 2022-0158-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-03-15
- Subjects:
- Blueberry -- Catechol oxidases -- Substrates -- Inhibitors
Food industry and trade -- Periodicals
Food -- Composition -- Periodicals
Microbiology -- Periodicals
Nutrition -- Periodicals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00236438 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.lwt.2022.113142 ↗
- Languages:
- English
- ISSNs:
- 0023-6438
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3983.070000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 20803.xml