Structure and biotechnological applications of odorant-binding proteins

被引:146
作者
Pelosi, Paolo [1 ]
Mastrogiacomo, Rosa [1 ]
Iovinella, Immacolata [1 ]
Tuccori, Elena [2 ]
Persaud, Krishna C. [2 ]
机构
[1] Univ Pisa, Dept Agr Food & Environm, I-56124 Pisa, Italy
[2] Univ Manchester, Sch Chem Engn & Analyt Sci, Manchester, Lancs, England
关键词
Odorant-binding proteins; Biosensors; Protein stability; Fluorescence binding; Electronic nose; PHEROMONE-BINDING; ELECTRONIC NOSES; INFRARED-SPECTROSCOPY; CHEMOSENSORY PROTEINS; ANTHERAEA-POLYPHEMUS; PERIRECEPTOR EVENTS; SEXUAL ATTRACTION; SOLUBLE-PROTEINS; SILKWORM MOTH; EXPRESSION;
D O I
10.1007/s00253-013-5383-y
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
Odorant-binding proteins (OBPs) are small soluble polypeptides found in sensory organs of vertebrates and insects as well as in secretory glands and are dedicated to detection and release of chemical stimuli. OBPs of vertebrates belong to the family of lipocalin proteins, while those of insects are folded into alpha-helical domains. Both types of architectures are extremely stable to temperature, organic solvents and proteolytic digestion. These characteristics make OBPs suitable elements for fabricating biosensors to be used in the environment, as well as for other biotechnological applications. The affinity of OBPs for small volatile organic compounds is in the micromolar range, and they have broad specificity to a range of ligands. For biotechnological applications, OBPs can be expressed in bacterial systems at low cost and are easily purified. The large amount of information available on their structures and affinities to different molecules should allow the design of specific mutants with desired characteristics and represent a solid base for tailoring OBPs for different applications.
引用
收藏
页码:61 / 70
页数:10
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