A novel amylolytic enzyme from Palaeococcus ferrophilus with malto-oligosaccharide forming ability belonging to subfamily GH13_20. (February 2022)
- Record Type:
- Journal Article
- Title:
- A novel amylolytic enzyme from Palaeococcus ferrophilus with malto-oligosaccharide forming ability belonging to subfamily GH13_20. (February 2022)
- Main Title:
- A novel amylolytic enzyme from Palaeococcus ferrophilus with malto-oligosaccharide forming ability belonging to subfamily GH13_20
- Authors:
- Ji, Hangyan
Li, Xiaoxiao
Jiang, Tong
Fang, Qi
Bai, Yuxiang
Long, Jie
Chen, Long
Jin, Zhengyu - Abstract:
- Abstract: By heterologous expression of a gene from Palaeococcus ferrophilus, a novel recombinant enzyme designated AMPf was obtained and proved to be an amylolytic enzyme with unique catalytic characteristics. The optimal temperature and pH of AMPf were 50 °C and 7.0 respectively. Although sequence analysis and acarbose hydrolysis ability indicated that AMPf belongs to the subfamily GH13_20, interestingly, this enzyme hardly acts on cyclodextrins and pullulan distinguishing it from most enzymes in this subfamily. AMPf hydrolyzes starches to glucose, maltose, maltotriose, and maltotetrose as main products. AMPf mainly liberates glucose from starch with the concentration of 1% (w/v), while it shows malto-oligosaccharide forming ability with higher starch concentration of 4% (w/v). Also, the 4, 6-ethylidene-4-nitrophenyl-maltoheptaose hydrolysis ability further indicates the unique combination endo-acting and glucose releasing exo-acting activtity of AMPf. AMPf could utilize maltose and maltotriose to produce malto-oligosaccharides by transglycosylation activity. It was proven AMPf has application protential in malto-oligosaccharides production. Graphical abstract: Image 1 Highlights: A novel amylolytic enzyme from Palaeococcus ferrophilus (AMPf) was discovered. AMPf was fully characterized and proved to be from subfamily GH13_20. AMPf was amylolytic enzyme with endo- and glucose releasing exo-acting activtity. AMPf mainly produced malto-oligosacchardes at high starchAbstract: By heterologous expression of a gene from Palaeococcus ferrophilus, a novel recombinant enzyme designated AMPf was obtained and proved to be an amylolytic enzyme with unique catalytic characteristics. The optimal temperature and pH of AMPf were 50 °C and 7.0 respectively. Although sequence analysis and acarbose hydrolysis ability indicated that AMPf belongs to the subfamily GH13_20, interestingly, this enzyme hardly acts on cyclodextrins and pullulan distinguishing it from most enzymes in this subfamily. AMPf hydrolyzes starches to glucose, maltose, maltotriose, and maltotetrose as main products. AMPf mainly liberates glucose from starch with the concentration of 1% (w/v), while it shows malto-oligosaccharide forming ability with higher starch concentration of 4% (w/v). Also, the 4, 6-ethylidene-4-nitrophenyl-maltoheptaose hydrolysis ability further indicates the unique combination endo-acting and glucose releasing exo-acting activtity of AMPf. AMPf could utilize maltose and maltotriose to produce malto-oligosaccharides by transglycosylation activity. It was proven AMPf has application protential in malto-oligosaccharides production. Graphical abstract: Image 1 Highlights: A novel amylolytic enzyme from Palaeococcus ferrophilus (AMPf) was discovered. AMPf was fully characterized and proved to be from subfamily GH13_20. AMPf was amylolytic enzyme with endo- and glucose releasing exo-acting activtity. AMPf mainly produced malto-oligosacchardes at high starch concentration. AMPf could use maltose and maltotriose to produce malto-oligosaccharides. … (more)
- Is Part Of:
- Food bioscience. Volume 45(2022)
- Journal:
- Food bioscience
- Issue:
- Volume 45(2022)
- Issue Display:
- Volume 45, Issue 2022 (2022)
- Year:
- 2022
- Volume:
- 45
- Issue:
- 2022
- Issue Sort Value:
- 2022-0045-2022-0000
- Page Start:
- Page End:
- Publication Date:
- 2022-02
- Subjects:
- Amylolytic enzyme -- Catalytic charateristics -- Malto-oligosaccharides -- Palaeococcus ferrophilus
Food -- Biotechnology -- Periodicals
Food -- Research -- Periodicals
Aliments -- Biotecnologia -- Revistes
Aliments -- Investigació -- Revistes
Food -- Biotechnology
Food -- Research
Revistes electròniques
Periodicals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/22124292 ↗
http://www.sciencedirect.com/ ↗ - DOI:
- 10.1016/j.fbio.2021.101498 ↗
- Languages:
- English
- ISSNs:
- 2212-4292
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 20347.xml