Recombinant expression, fermentation and characterization of a type Ⅲ human like collagen

XIANG Zhixiang; GONG Jingsong; XU Zhenghong; SHI Jingsong

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Recombinant expression, fermentation and characterization of a type Ⅲ human like collagen

XIANG Zhixiang 1,GONG Jingsong 1 *,XU Zhenghong 2,SHI Jingsong 1

1.Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, PR China;Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, PR China;National Engineering Research Center for Cereal Fermentation and Food Biomanufacturing, School of Biotechnology, Jiangnan University, Wuxi 214122, PR China;Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Life Sciences and Health Engineering, Jiangnan University, Wuxi 214122, PR China

2.National Engineering Research Center for Cereal Fermentation and Food Biomanufacturing, School of Biotechnology, Jiangnan University, Wuxi 214122, PR China

*Correspondence author

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Funding: National Natural Science Foundation of China （No.No. 21978116 and 32171261）, Fundamental Research Funds for the Central Universities （No.No. JUSRP22047）

Opened online:17 May 2022

Accepted by: none

Citation: XIANG Zhixiang,GONG Jingsong,XU Zhenghong.Recombinant expression, fermentation and characterization of a type Ⅲ human like collagen[OL]. [17 May 2022] http://en.paper.edu.cn/en_releasepaper/content/4757718

Collagen, the highest content protein in the body, as irreplaceable biological functions, and it is widespread concerned in food, beauty, and medicine with great market demand. The gene encoding hlCOLⅢ α1 chain fragment was integrated into Pichia pastoris genome after partial amino acids were substituted. Combined with promoter engineering and high-density fermentation technology, soluble secretory expression with the highest yield of 1.05 g L-1 was achieved using two-stage feeding method, and the purity could reach 96% after affinity purification. The determination of N/C-terminal protein sequence were consistent with the theoretical expectation, glycine shared 27.02% and proline 23.92% in amino acid analysis, which were in accordance with the characteristics of collagen. Mass spectrometry combined with Fourier transform infrared spectroscopy and circular dichroism revealed that the target product existed as homologous dimer and trimer in the broth , which laid a foundation for exploring the self-assembly of collagen.

Keywords:human-like collagen, secretory expression, fermentation, protein purification, characterization

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