Coix lacryma-jobi chymotrypsin inhibitor displays antifungal activity.
Pestic Biochem Physiol
; 160: 49-57, 2019 Oct.
Article
em En
| MEDLINE
| ID: mdl-31519257
ABSTRACT
A novel chymotrypsin inhibitor, named ClCI, was purified from coix seed (Coix lacryma-jobi L.) by aqueous two-phase extraction, chymotrypsin-Sepharose 4B affinity chromatography and centrifugal ultrafiltration. ClCI was a 7.9â¯kDa competitive inhibitor with pI 6.54. The inhibition constants (Ki) for bovine pancreatic chymotrypsin and bacterial subtilisin were 1.27â¯×â¯10-10â¯M and 1.57â¯×â¯10-9â¯M respectively. ClCI had no inhibitory activity against bovine trypsin and porcine elastase. ClCI had wide pH stability and good heat resistance. It can maintain >90% inhibition activity against chymotrypsin at 20-80⯰C for 1â¯h. The primary structure of ClCI was highly similar (57%-92%) to those of several inhibitors belonging to the Gramineae crop potato protease inhibitor- I superfamily and showed the typical sequence motif of the protease inhibitor of the seed storage protein group. ClCI (12.5â¯mg) inhibited mycelial growth of the phytopathogenic fungi Mycosphaerella melonis, Helminthosporium turcicum, Alternaria solani, Phytophthora capsici, Isariopsis griseola, and Colletotrichum gloeosporioides, and caused 89% inhibition of the proteases from spore germination of plant-pathogenic fungi. The results of the present study indicate that ClCI had biotechnological potential as an alternative agent to combat the important phytopathogenic fungi.
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MEDLINE
Assunto principal:
Quimotripsina
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Inibidores da Tripsina
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Coix
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Antifúngicos
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article