Cloning and characteristic prediction of 42 kda chitinase from trichoderma asperellum
Vol. 130 No. 1C (2021), Original Article
Vol. 130 No. 1C (2021)

Cloning and characteristic prediction of 42 kda chitinase from trichoderma asperellum

Original Article
https://doi.org/10.26459/hueunijns.v130i1C.6275
Published 2021-09-30
Phung Thi Bich Hoa
Faculty of Biology, University of Education, Hue University, 34 Le Loi St., Hue, Viet Nam
Mai Thi Thu Hien
Le Loi Secondary school, Ngu Hanh Son, Da Nang
Nguyen Hoang Tue
Faculty of Biology, University of Sciences, Hue University, 77 Nguyen Hue St., Hue, Vietnam
Nguyen Ty
Faculty of Biology, University of Education, Hue University, 34 Le Loi St., Hue, Viet Nam
Nguyen Thi Kim Co
Faculty of Biology, University of Education, Hue University, 34 Le Loi St., Hue, Viet Nam
Nguyen Xuan Huy*
Hue University, 03 Le Loi St. Hue, Vietnam
PDF (Vietnamese)

Keywords

Chitinase 42 kDa
cloning
characteristic Chitinase 42 kDa
đặc tính
tạo dòng
Trichoderma asperellum

How to Cite

1.
Phùng TBH, Mai TTH, Nguyễn HT, Nguyễn T, Nguyễn TKC, Nguyễn XH. Cloning and characteristic prediction of 42 kda chitinase from trichoderma asperellum. hueuni-jns [Internet]. 2021Sep.30 [cited 2024Nov.22];130(1C):105-12. Available from: https://jos.hueuni.edu.vn/index.php/hujos-ns/article/view/6275
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Abstract

Chitinase is an enzyme that catalyzes the hydrolytic reaction of chitin by cleaving 1,4-N-acetyl-β-glucosaminide linkages. Chitinase has been widely used in various fields, especially pest control, pollution reduction, and basic and applied biology. Chitinase from microorganisms is an essential source, typically from Trichoderma. After removing intron sequences, the gene encoding chitinase 42 kDa (chi42) from Trichoderma asperellum SH16 was synthesized and cloned into the pUC19 vector. The gene chi42 digested by BamHI and SacI was successfully cloned into the pQE30 vector, which was expressed in E. coli. The primary in silico analysis of the protein structure shows that chitinase is an extracellular protein. The secondary structure analysis reveals that chitinase has 15 α helices and 13 β sheets, while the dimension structure of chitinase is highly homological with the chitin hydrolytic enzyme from T. harzianum. The chitinase from T. asperellum is resistant to temperatures higher than 65 °C and exhibits acidic catalysis activity. Our results would provide basic information for heterologous expression and scale-up production of chitinase 42 kDa.

https://doi.org/10.26459/hueunijns.v130i1C.6275
PDF (Vietnamese)

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