A novel enzyme from Rhodotorula mucilaginosa Aldolase: Isolation, identification and degradation for patulin in apple juice. (May 2022)
- Record Type:
- Journal Article
- Title:
- A novel enzyme from Rhodotorula mucilaginosa Aldolase: Isolation, identification and degradation for patulin in apple juice. (May 2022)
- Main Title:
- A novel enzyme from Rhodotorula mucilaginosa Aldolase: Isolation, identification and degradation for patulin in apple juice
- Authors:
- Li, Na
Cui, Rui
Zhang, Fang
Meng, Xianghong
Liu, Bingjie - Abstract:
- Abstract: Patulin is a mycotoxin produced by Penicillium species that can cause severe food safety concerns. Biological enzymes are considered one of the promising methods for degrading patulin. The purpose of this study was focused on isolating and purifying Aldolase from Rhodotorula mucilaginosa . The results showed that the molecular weight of purified Aldolase was 36 kDa. The Aldolase had an optimal pH 7.0 and was stable at a pH range of 5.5–7.0. The optimum temperature for Aldolase was 25 °C and exhibited thermostability in the range of 4–25 °C. The Aldolase activity was induced moderately by Ca 2+, Cu 2+, PMSF and SDS, while Fe 3+ and EDTA significantly inhibited the activity. The kinetic parameters ( K m and V max ) for Aldolase were 109.46 mM and 4.34 mM/h, respectively. When 0.7 mg/mL of Aldolase was added, 2 mg/L of patulin in apple juice can be degraded. Moreover, there is no significant difference in the quality parameters and volatile compounds before and after degradation in apple juice. Finally, the Aldolase gene was successfully cloned and expressed in E. coli . Meanwhile, the purified cloned Aldolase has an excellent patulin degradation ratio of more than 99% (15 mg/L). These findings suggested that Aldolase was a promising material for patulin degradation. Graphical Abstract: ga1 Highlights: Aldolase has been isolated and identified from Rhodotorula mucilaginosa . Adding 0.7 mg/mL Aldolase could reduce 2 mg/L patulin at 25 °C for 36 h. The degradationAbstract: Patulin is a mycotoxin produced by Penicillium species that can cause severe food safety concerns. Biological enzymes are considered one of the promising methods for degrading patulin. The purpose of this study was focused on isolating and purifying Aldolase from Rhodotorula mucilaginosa . The results showed that the molecular weight of purified Aldolase was 36 kDa. The Aldolase had an optimal pH 7.0 and was stable at a pH range of 5.5–7.0. The optimum temperature for Aldolase was 25 °C and exhibited thermostability in the range of 4–25 °C. The Aldolase activity was induced moderately by Ca 2+, Cu 2+, PMSF and SDS, while Fe 3+ and EDTA significantly inhibited the activity. The kinetic parameters ( K m and V max ) for Aldolase were 109.46 mM and 4.34 mM/h, respectively. When 0.7 mg/mL of Aldolase was added, 2 mg/L of patulin in apple juice can be degraded. Moreover, there is no significant difference in the quality parameters and volatile compounds before and after degradation in apple juice. Finally, the Aldolase gene was successfully cloned and expressed in E. coli . Meanwhile, the purified cloned Aldolase has an excellent patulin degradation ratio of more than 99% (15 mg/L). These findings suggested that Aldolase was a promising material for patulin degradation. Graphical Abstract: ga1 Highlights: Aldolase has been isolated and identified from Rhodotorula mucilaginosa . Adding 0.7 mg/mL Aldolase could reduce 2 mg/L patulin at 25 °C for 36 h. The degradation process of Aldolase has no deterioration on quality of apple juice. Aldolase gene was successfully cloned and expressed in Escherichia coli . … (more)
- Is Part Of:
- Process biochemistry. Volume 116(2022)
- Journal:
- Process biochemistry
- Issue:
- Volume 116(2022)
- Issue Display:
- Volume 116, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 116
- Issue:
- 2022
- Issue Sort Value:
- 2022-0116-2022-0000
- Page Start:
- 148
- Page End:
- 156
- Publication Date:
- 2022-05
- Subjects:
- Aldolase -- Isolation -- Identification -- Degradation -- Patulin -- Apple juice
Biochemical engineering -- Periodicals
Biotechnology -- Periodicals
Biochemistry -- periodicals
Biotechnology -- periodicals
Chemical Engineering -- periodicals
Génie biochimique -- Périodiques
Biotechnologie -- Périodiques
Biochemical engineering
Biotechnology
Periodicals
660.63 - Journal URLs:
- http://www.sciencedirect.com/science/journal/13595113 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.procbio.2022.03.001 ↗
- Languages:
- English
- ISSNs:
- 1359-5113
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 6849.983500
British Library DSC - BLDSS-3PM
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- 21223.xml