FOOD SCIENCE ›› 2021, Vol. 42 ›› Issue (8): 98-105.doi: 10.7506/spkx1002-6630-20200819-248

• Bioengineering • Previous Articles     Next Articles

High-level Expression, Characterization, and Application of a Novel β-Mannanase from Penicillium chrysogenum

ZHEN Hongmin, HUA Xiaohan, MA Junwen, WEN Yongping, LI Yanxiao, YAN Qiaojuan, JIANG Zhengqiang   

  1. (1. College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China; 2. College of Engineering, China Agricultural University, Beijing 100083, China; 3. Meng Niu Hi-Tech Dairy (Beijing) Co. Ltd., Beijing 100101, China)
  • Online:2021-04-25 Published:2021-05-14

Abstract: A cloned β-mannanase (PcMan26A) gene from Penicillium chrysogenum was successfully expressed in Penicillium chrysogenum. At the end of high cell density fermentation, the enzymatic activity of the fermentation supernatant reached 25 200 U/mL. The enzyme belonged to the glycoside hydrolase family 26 and shared the highest amino acid sequence identity (67.8%) with β-mannanase from Aspergillus niger CBS 513.88. The optimal reaction conditions for PcMan26A were pH 6.0 and 50 ℃, and it was stable at 45 ℃ and within a broad pH range of 4.0–8.0. The enzyme showed the highest specific activity (3 581.0 U/mg) towards konjac powder. Furthermore, PcMan26A was used for konjac powder hydrolysis, yielding konjac manno-oligosaccharide with a yield of 86.2%. The main composition of the konjac manno-oligosaccharide was manno-oligosaccharides with degree of polymerization > 4. The recombinant β-mannanase provides a new option for the enzymatic production of konjac manno-oligosaccharide.

Key words: Penicillium chrysogenum; β-mannanase; Pichia pastoris; konjac powder; manno-oligosaccharide

CLC Number: