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Effect of ß-mannanase domain from Trichoderma reesei on its biochemical characters and synergistic hydrolysis of sugarcane bagasse.
Ma, Lijuan; Ma, Qing; Cai, Rui; Zong, Zhiyou; Du, Liping; Guo, Gaojie; Zhang, Yingying; Xiao, Dongguang.
Afiliación
  • Ma L; Key Laboratory of Industrial Microbiology, Ministry of Education, Tianjin Industrial Microbiology Key Laboratory, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
  • Ma Q; Key Laboratory of Industrial Microbiology, Ministry of Education, Tianjin Industrial Microbiology Key Laboratory, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
  • Cai R; Key Laboratory of Industrial Microbiology, Ministry of Education, Tianjin Industrial Microbiology Key Laboratory, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
  • Zong Z; State Key Laboratory of Medicinal Chemical Biology, Nankai University, Tianjin, China.
  • Du L; Key Laboratory of Industrial Microbiology, Ministry of Education, Tianjin Industrial Microbiology Key Laboratory, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
  • Guo G; Key Laboratory of Industrial Microbiology, Ministry of Education, Tianjin Industrial Microbiology Key Laboratory, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
  • Zhang Y; Key Laboratory of Industrial Microbiology, Ministry of Education, Tianjin Industrial Microbiology Key Laboratory, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
  • Xiao D; Key Laboratory of Industrial Microbiology, Ministry of Education, Tianjin Industrial Microbiology Key Laboratory, College of Biotechnology, Tianjin University of Science and Technology, Tianjin, China.
J Sci Food Agric ; 98(7): 2540-2547, 2018 May.
Article en En | MEDLINE | ID: mdl-29028116
BACKGROUND: ß-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 ß-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 (Km = 2.5 mg mL-1 ) than Man1 (Km = 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.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Trichoderma / Proteínas Fúngicas / Saccharum / Beta-Manosidasa Idioma: En Revista: J Sci Food Agric Año: 2018 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Trichoderma / Proteínas Fúngicas / Saccharum / Beta-Manosidasa Idioma: En Revista: J Sci Food Agric Año: 2018 Tipo del documento: Article País de afiliación: China Pais de publicación: Reino Unido