Chitinase system ofAeromonas salmonicida, and characterization of enzymes involved in chitin degradation

被引:24
作者
Pentekhina, Iuliia [1 ,2 ]
Hattori, Tatsuyuki [1 ]
Dinh Minh Tran [3 ]
Shima, Mizuki [4 ]
Watanabe, Takeshi [1 ,4 ,6 ]
Sugimoto, Hayuki [1 ,4 ]
Suzuki, Kazushi [1 ,4 ,5 ]
机构
[1] Niigata Univ, Grad Sch Sci & Technol, Niigata, Japan
[2] Far Eastern Fed Univ, Sch Econ & Management, Vladivostok, Russia
[3] Tay Nguyen Univ, Inst Biotechnol & Environm, Buon Ma Thuot, Vietnam
[4] Niigata Univ, Fac Agr, Dept Appl Biol Chem, Niigata, Japan
[5] Niigata Univ, Sakeol Ctr, Niigata, Japan
[6] Niigata Agrofood Univ, Fac Agrofood Sci, Niigata, Japan
关键词
Aeromonas salmonicida; chitinase; lytic polysaccharide monooxygenase; synergistic effect; antifungal activity; FAMILY; 19; CHITINASE; BINDING DOMAIN; LOOP STRUCTURE; CLONING; IDENTIFICATION; EXPRESSION; BACTERIUM; SEQUENCE; STRAIN; GENE;
D O I
10.1080/09168451.2020.1771539
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The genes encoding chitin-degrading enzymes inAeromonas salmonicidaSWSY-1.411 were identified and cloned inEscherichia coli. The strain contained two glycoside hydrolase (GH) families 18 chitinases: AsChiA and AsChiB, two GH19 chitinases: AsChiC and AsChiD, and an auxiliary activities family 10 protein, lytic polysaccharide monooxygenase: AsLPMO10A. These enzymes were successfully expressed inE. coliand purified. AsChiB had the highest hydrolytic activity against insoluble chitin. AsChiD had the highest activity against water-soluble chitin. The peroxygenase activity of AsLPMO10A was lower compared to SmLPMO10A fromSerratia marcescens. Synergism on powdered chitin degradation was observed when AsChiA and AsLPMO10A were combined with other chitinases of this strain. More than twice the increase of the synergistic effect was observed when powdered chitin was treated by a combination of AsLPMO10A with all chitinases. GH19 chitinases suppressed the hyphal growth ofTrichoderma reesei.
引用
收藏
页码:1936 / 1947
页数:12
相关论文
共 60 条
[1]   Identification of the substrate interaction region of the chitin-binding domain of Streptomyces griseus chitinase C [J].
Akagi, K ;
Watanabe, J ;
Hara, M ;
Kezuka, Y ;
Chikaishi, E ;
Yamaguchi, T ;
Akutsu, H ;
Nonaka, T ;
Watanabe, T ;
Ikegami, T .
JOURNAL OF BIOCHEMISTRY, 2006, 139 (03) :483-493
[2]   Heterologous expression and characterization of wild-type and mutant forms of a 26 kDa endochitinase from barley (Hordeum vulgare L) [J].
Andersen, MD ;
Jensen, A ;
Robertus, JD ;
Leah, R ;
Skriver, JK .
BIOCHEMICAL JOURNAL, 1997, 322 :815-822
[3]  
[Anonymous], 2017, J ONCOL PRACT, V13, pe353
[4]  
BERGER LR, 1958, BIOCHIM BIOPHYS ACTA, V29, P522
[5]   The role of enzyme distortion in the single displacement mechanism of family 19 chitinases [J].
Brameld, KA ;
Goddard, WA .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (08) :4276-4281
[6]   Substrate assistance in the mechanism of family 18 chitinases: Theoretical studies of potential intermediates and inhibitors [J].
Brameld, KA ;
Shrader, WD ;
Imperiali, B ;
Goddard, WA .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 280 (05) :913-923
[7]   A fast and sensitive activity assay for lytic polysaccharide monooxygenase [J].
Breslmayr, Erik ;
Hanzek, Marija ;
Hanrahan, Aoife ;
Leitner, Christian ;
Kittl, Roman ;
Santek, Bozidar ;
Oostenbrink, Chris ;
Ludwig, Roland .
BIOTECHNOLOGY FOR BIOFUELS, 2018, 11
[8]   Genome sequence of the nematode C-elegans:: A platform for investigating biology [J].
不详 .
SCIENCE, 1998, 282 (5396) :2012-2018
[9]  
Collinge DB, 1993, PLANT J, V3
[10]  
Tran DM, 2018, BIOSCI BIOTECH BIOCH, V82, P343, DOI [10.1080/09168451.2017.1422969, 10.1080/09168451.2017.142]