| Literature DB >> 18020416 |
Railene de Azevedo Pereira1, Arnubio Valencia-Jiménez, Cláudio Picanço Magalhães, Maura Vianna Prates, Jorge Alex Taquita Melo, Liziane Maria de Lima, Maurício Pereira de Sales, Erich Yukio Tempel Nakasu, Maria Cristina Mattar da Silva, Maria Fátima Grossi-de-Sá.
Abstract
The coffee berry borer, Hypothenemus hampei (Ferrari), is an important devastating coffee pest worldwide. Both trypsin and chymotrypsin enzyme activities from H. hampei larval midgut can be inactivated by proteinaceous enzyme-inhibitors. A serine proteinase inhibitor belonging to the Bowman-Birk class was purified from a wild accession of Phaseolus coccineus L. seeds. The inhibitor (PcBBI1) is a cysteine-rich protein that is heat-stable at alkaline pH. MALDI-TOF/MS analysis showed that PcBBI1 occurs in seeds as a monomer (8689 Da) or dimer (17,378 Da). Using in vitro inhibition assays, it was found that PcBBI1 has a high inhibitory activity against H. hampei trypsin-like enzymes, bovine pancreatic chymotrypsin, and trypsin. According to this, PcBBI1 could be a promising tool to make genetically modified coffee with resistance to coffee berry borer.Entities:
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Year: 2007 PMID： 18020416 DOI： 10.1021/jf072155x
Source DB: PubMed Journal: J Agric Food Chem ISSN： 0021-8561 Impact factor: 5.279