Biotechnological approaches to develop bacterial chitinases as a bioshield against fungal diseases of plants

被引:95
作者
Neeraja, Chilukoti [1 ]
Anil, Kondreddy [1 ]
Purushotham, Pallinti [1 ]
Suma, Katta [1 ]
Sarma, P. V. S. R. N. [1 ]
Moerschbacher, Bruno M. [2 ]
Podile, Appa Rao [1 ]
机构
[1] Univ Hyderabad, Dept Plant Sci, Hyderabad 500046, Andhra Pradesh, India
[2] Univ Munster, Inst Plant Biochem & Biotechnol, Munster, Germany
关键词
Biocontrol; chitinolytic bacteria; chitinases; fungal pathogens; chitin; EXPOSED AROMATIC RESIDUES; BACILLUS-CIRCULANS WL-12; AEROMONAS-CAVIAE CB101; LATE LEAF-SPOT; BIOLOGICAL-CONTROL; SERRATIA-MARCESCENS; BINDING DOMAIN; ANTIFUNGAL ACTIVITY; DIRECTED EVOLUTION; BIOCHEMICAL-CHARACTERIZATION;
D O I
10.3109/07388551.2010.487258
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Fungal diseases of plants continue to contribute to heavy crop losses in spite of the best control efforts of plant pathologists. Breeding for disease-resistant varieties and the application of synthetic chemical fungicides are the most widely accepted approaches in plant disease management. An alternative approach to avoid the undesired effects of chemical control could be biological control using antifungal bacteria that exhibit a direct action against fungal pathogens. Several biocontrol agents, with specific fungal targets, have been registered and released in the commercial market with different fungal pathogens as targets. However, these have not yet achieved their full commercial potential due to the inherent limitations in the use of living organisms, such as relatively short shelf life of the products and inconsistent performance in the field. Different mechanisms of action have been identified in microbial biocontrol of fungal plant diseases including competition for space or nutrients, production of antifungal metabolites, and secretion of hydrolytic enzymes such as chitinases and glucanases. This review focuses on the bacterial chitinases that hydrolyze the chitinous fungal cell wall, which is the most important targeted structural component of fungal pathogens. The application of the hydrolytic enzyme preparations, devoid of live bacteria, could be more efficacious in fungal control strategies. This approach, however, is still in its infancy, due to prohibitive production costs. Here, we critically examine available sources of bacterial chitinases and the approaches to improve enzymatic properties using biotechnological tools. We project that the combination of microbial and recombinant DNA technologies will yield more effective environment-friendly products of bacterial chitinases to control fungal diseases of crops.
引用
收藏
页码:231 / 241
页数:11
相关论文
共 105 条
[51]   Chitin-supplemented formulations improve biocontrol and plant growth promoting efficiency of Bacillus subtilis AF 1 [J].
Manjula, K ;
Podile, AR .
CANADIAN JOURNAL OF MICROBIOLOGY, 2001, 47 (07) :618-625
[52]   Cold adaptation of a psychrophilic chitinase: a mutagenesis study [J].
Mavromatis, K ;
Feller, G ;
Kokkinidis, M ;
Bouriotis, V .
PROTEIN ENGINEERING, 2003, 16 (07) :497-503
[53]   Aeromonas caviae CB101 Contains Four Chitinases Encoded by a Single Gene chi1 [J].
Mehmood, Muhammad Aamer ;
Gai, Yingbao ;
Zhuang, Qunchuan ;
Wang, Feng ;
Xiao, Xiang ;
Wang, Fengping .
MOLECULAR BIOTECHNOLOGY, 2010, 44 (03) :213-220
[54]   Purification and characterization of a chitinase from Serratia proteamaculans [J].
Mehmood, Muhammad Aamer ;
Xiao, Xiang ;
Hafeez, Fauzia Yusuf ;
Gai, Yingbao ;
Wang, Fengping .
WORLD JOURNAL OF MICROBIOLOGY & BIOTECHNOLOGY, 2009, 25 (11) :1955-1961
[55]  
Mondal KC, 2000, J BASIC MICROB, V40, P223, DOI 10.1002/1521-4028(200008)40:4<223::AID-JOBM223>3.0.CO
[56]  
2-L
[57]   Swapping the chitin-binding domain in Bacillus chitinases improves the substrate binding affinity and conformational stability [J].
Neeraja, Chilukoti ;
Subramanyam, Rajagopal ;
Moerschbacher, Bruno M. ;
Podile, Appa Rao .
MOLECULAR BIOSYSTEMS, 2010, 6 (08) :1492-1502
[58]   Fusion of cellulose binding domain to the catalytic domain improves the activity and conformational stability of chitinase in Bacillus licheniformis DSM13 [J].
Neeraja, Chilukoti ;
Moerschbacher, Bruno ;
Podile, Appa Rao .
BIORESOURCE TECHNOLOGY, 2010, 101 (10) :3635-3641
[59]  
Pantoom Supansa, 2008, BMC Biochemistry, V9, P2, DOI 10.1186/1471-2091-9-2
[60]   Chitinolytic enzymes: an exploration [J].
Patil, RS ;
Ghormade, V ;
Deshpande, MV .
ENZYME AND MICROBIAL TECHNOLOGY, 2000, 26 (07) :473-483