Characterization of a thermostable glycoside hydrolase (CMbg0408) from the hyperthermophilic archaeon Caldivirga maquilingensis IC‐167. (28th September 2016)
- Record Type:
- Journal Article
- Title:
- Characterization of a thermostable glycoside hydrolase (CMbg0408) from the hyperthermophilic archaeon Caldivirga maquilingensis IC‐167. (28th September 2016)
- Main Title:
- Characterization of a thermostable glycoside hydrolase (CMbg0408) from the hyperthermophilic archaeon Caldivirga maquilingensis IC‐167
- Authors:
- Letsididi, Rebaone
Hassanin, Hinawi AM
Koko, Marwa YF
Ndayishimiye, Jean B
Zhang, Tao
Jiang, Bo
Stressler, Timo
Fischer, Lutz
Mu, Wanmeng - Abstract:
- Abstract: BACKGROUND: Hyperthermophilic archaea capable of functioning optimally at very high temperatures are a good source of unique and industrially important thermostable enzymes. RESULTS: A glycoside hydrolase family 1 β‐galactosidase gene ( Bgl B) from a hyperthermophilic archaeon Caldivirga maquilingensis IC‐167 was cloned and expressed in Escherichia coli . The recombinant enzyme (CMbg0408) displayed optimum activity at 110 °C and pH 5.0. It also retained 92% and 70% of its maximal activity at 115 and 120 °C, respectively. The enzyme was completely thermostable and active after 120 min of incubation at 80 and 90 °C. It also showed broad substrate specificity with activities of 8876 ± 185 U mg −1 for p ‐nitrophenyl‐β‐d ‐galactopyranoside, 4464 ± 172 U mg −1 for p ‐nitrophenyl‐β‐d ‐glucopyranoside, 1486 ± 68 U mg −1 for o‐nitrophenyl‐β‐d ‐galactopyranoside, 2250 ± 86 U mg −1 for o ‐nitrophenyl‐β‐d ‐xylopyranoside and 175 ± 4 U mg −1 for lactose. A catalytic efficiency ( k cat / K m ) of 3059 ± 122 mmol L −1 s −1 and K m value of 8.1 ± 0.08 mmol L −1 were displayed towards p ‐nitrophenyl‐β‐d ‐galactopyranoside. CONCLUSION: As a result of its remarkable thermostability and high activity at high temperatures, this novel β‐galactosidase may be useful for food and pharmaceutical applications. © 2016 Society of Chemical Industry
- Is Part Of:
- Journal of the science of food and agriculture. Volume 97:Number 7(2017)
- Journal:
- Journal of the science of food and agriculture
- Issue:
- Volume 97:Number 7(2017)
- Issue Display:
- Volume 97, Issue 7 (2017)
- Year:
- 2017
- Volume:
- 97
- Issue:
- 7
- Issue Sort Value:
- 2017-0097-0007-0000
- Page Start:
- 2132
- Page End:
- 2140
- Publication Date:
- 2016-09-28
- Subjects:
- β‐galactosidase -- glycoside hydrolase -- hyperthermophilic -- Caldivirga maquilingensis -- thermostability
Food -- Periodicals
Agriculture -- Periodicals
664 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)1097-0010 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/jsfa.8019 ↗
- Languages:
- English
- ISSNs:
- 0022-5142
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5055.000000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 755.xml