Effect of β‐mannanase domain from Trichoderma reesei on its biochemical characters and synergistic hydrolysis of sugarcane bagasse. (13th November 2017)
- Record Type:
- Journal Article
- Title:
- Effect of β‐mannanase domain from Trichoderma reesei on its biochemical characters and synergistic hydrolysis of sugarcane bagasse. (13th November 2017)
- Main Title:
- Effect of β‐mannanase domain from Trichoderma reesei on its biochemical characters and synergistic hydrolysis of sugarcane bagasse
- Authors:
- Ma, Lijuan
Ma, Qing
Cai, Rui
Zong, Zhiyou
Du, Liping
Guo, Gaojie
Zhang, Yingying
Xiao, Dongguang - Abstract:
- Abstract: BACKGROUND: β ‐mannanase is a key enzyme for hydrolyzing mannan, a major constituent of hemicellulose, which is the second most abundant polysaccharide in nature. Different structural domains greatly affect its biochemical characters and catalytic efficiency. However, the effects of linker and carbohydrate‐binding module (CBM) on β ‐mannanase from Trichoderma reesei (Man1) have not yet been fully described. The present study aimed to determine the influence of different domains on the expression efficiency, biochemical characteristics and hemicellulosic deconstruction of Man1. RESULTS: The expression efficiency was improved after truncating CBM. Activities of Man1 and Man1ΔCBM (CBM) in the culture supernatant after 168 h of induction were 34.5 and 42.9 IU mL –1, although a value of only 0.36 IU mL –1 was detected for Man1ΔLCBM (lacking CBM and linker). Man1 showed higher thermostability than Man1ΔCBM at low temperature, whereas Man1ΔCBM had a higher specificity for galactomannan ( K m = 2.5 mg mL –1 ) than Man1 ( K m = 4.0 mg mL –1 ). Both Man1 and Man1ΔCBM could synergistically improve the hydrolysis of cellulose, galactomannan and pretreated sugarcane bagasse, with a 10–30% improvement of the reducing sugar yield. CONCLUSION: Linker and CBM domains were vital for mannanase activity and expression efficiency. CBM affected the thermostability and adsorption ability of Man1. The results obtained in the present study should help guide the rational design andAbstract: BACKGROUND: β ‐mannanase is a key enzyme for hydrolyzing mannan, a major constituent of hemicellulose, which is the second most abundant polysaccharide in nature. Different structural domains greatly affect its biochemical characters and catalytic efficiency. However, the effects of linker and carbohydrate‐binding module (CBM) on β ‐mannanase from Trichoderma reesei (Man1) have not yet been fully described. The present study aimed to determine the influence of different domains on the expression efficiency, biochemical characteristics and hemicellulosic deconstruction of Man1. RESULTS: The expression efficiency was improved after truncating CBM. Activities of Man1 and Man1ΔCBM (CBM) in the culture supernatant after 168 h of induction were 34.5 and 42.9 IU mL –1, although a value of only 0.36 IU mL –1 was detected for Man1ΔLCBM (lacking CBM and linker). Man1 showed higher thermostability than Man1ΔCBM at low temperature, whereas Man1ΔCBM had a higher specificity for galactomannan ( K m = 2.5 mg mL –1 ) than Man1 ( K m = 4.0 mg mL –1 ). Both Man1 and Man1ΔCBM could synergistically improve the hydrolysis of cellulose, galactomannan and pretreated sugarcane bagasse, with a 10–30% improvement of the reducing sugar yield. CONCLUSION: Linker and CBM domains were vital for mannanase activity and expression efficiency. CBM affected the thermostability and adsorption ability of Man1. The results obtained in the present study should help guide the rational design and directional modification of Man with respect to improving its catalytic efficiency. © 2017 Society of Chemical Industry … (more)
- Is Part Of:
- Journal of the science of food and agriculture. Volume 98:Number 7(2018)
- Journal:
- Journal of the science of food and agriculture
- Issue:
- Volume 98:Number 7(2018)
- Issue Display:
- Volume 98, Issue 7 (2018)
- Year:
- 2018
- Volume:
- 98
- Issue:
- 7
- Issue Sort Value:
- 2018-0098-0007-0000
- Page Start:
- 2540
- Page End:
- 2547
- Publication Date:
- 2017-11-13
- Subjects:
- mannanase -- structural domain -- biochemical characters -- thermostability -- Trichoderma reesei -- sugarcane bagasse
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.8741 ↗
- 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:
- 6335.xml