A novel endo-acting β-1,3-glucanase from Mesoflavibacter zeaxanthinifaciens S86: molecular characterization and biochemical properties

Title
A novel endo-acting β-1,3-glucanase from Mesoflavibacter zeaxanthinifaciens S86: molecular characterization and biochemical properties
Author(s)
이영득; 조은영; 강도형; 오철홍
KIOST Author(s)
Lee, Youngdeuk(이영득)Jo, Eunyoung(조은영)Kang, Do-Hyung(강도형)Oh, Chulhong(오철홍)
Publication Year
2016-11-10
Abstract
Glucanases are enzymes involve in degradation of glucans. Herein, a novel endo-β-1,3-glucanase counterpart, Mzl86 was identified from Mesoflavibacter Zeaxanthinifaciens S86. The deduced amino acid sequence of Mzl86 showed highest similarity (45.1%) with Leeuwenhoekiella blandensi and belongs to glycosyl hydrolase family 16. The Mzl86 was overexpressed in E. coli BL21 (DE3) and purified using His tag fusion protein purification system. Purified recombinant protein (rMz186) demonstrated a detectable enzymatic activity against laminarin with an optimum temperature and pH of 50°C and 8, respectively. The enzyme was stable at 50°C for 1 hour (demonstrating 80% of its maximum activity) and it was strongly activated in presence of 2.5 mM of manganese. Substrates specific activities of rMzl86 were found to be 261±9, 128±6 and 115±5 unit/mg against laminarin, barley β-glucan and lichenan, respectively. rMzl86 could degrades laminarioligosaccharides (lager than biose) and laminarin while producing mainly biose and glucose. Molecular characteristics and biochemical properties reveal that rMzl86 resembles the typical features of β-1,3-glucanase (EC 3.2.1.39) and is a potential good candidate to use in several industries such as agriculture, drug, chemical and bioethanol industries.y (45.1%) with Leeuwenhoekiella blandensi and belongs to glycosyl hydrolase family 16. The Mzl86 was overexpressed in E. coli BL21 (DE3) and purified using His tag fusion protein purification system. Purified recombinant protein (rMz186) demonstrated a detectable enzymatic activity against laminarin with an optimum temperature and pH of 50°C and 8, respectively. The enzyme was stable at 50°C for 1 hour (demonstrating 80% of its maximum activity) and it was strongly activated in presence of 2.5 mM of manganese. Substrates specific activities of rMzl86 were found to be 261±9, 128±6 and 115±5 unit/mg against laminarin, barley β-glucan and lichenan, respectively. rMzl86 could degrades laminarioligosaccharides (lager than biose) and laminarin while producing mainly biose and glucose. Molecular characteristics and biochemical properties reveal that rMzl86 resembles the typical features of β-1,3-glucanase (EC 3.2.1.39) and is a potential good candidate to use in several industries such as agriculture, drug, chemical and bioethanol industries.
URI
https://sciwatch.kiost.ac.kr/handle/2020.kiost/24338
Bibliographic Citation
International Conference of the Genetics Society of Korea 2016, pp.216, 2016
Publisher
The Genetics Society of Korea
Type
Conference
Language
English
Publisher
The Genetics Society of Korea
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