Biological Control of Pink Bollworm Pectinophora gossypiella (Saunders) by protease and Lipase Enzymes Produced from Streptomyces vinaceusdrappus SA (AB857336) | ||
| Egyptian Journal of Botany | ||
| Article 6, Volume 54, Issue 2, December 2014, Pages 263-279 PDF (738.71 K) | ||
| Document Type: Regular issue (Original Article) | ||
| DOI: 10.21608/ejbo.2014.491 | ||
| Abstract | ||
| TREPTOMYCES vinaceusdrappus SA was subjected to …...submerged fermentation under optimum conditions, at 30C and pH 7.0 in presence of 1% casein & 0.5% maltose and 0.5 % yeast & 1% sucrose for 6 and 5 days for protease and lipase production, respectively, under static conditions. Partial purification of protease and lipase were carried out by70% ammonium sulphate precipitation, dialysis, Sephadex G100 and finally Sephadex G50. The specific activities of protease and lipase at final purification step were 116.7 and 104.9 U mg-1 protein compared to 8.4 and 8.9 U mg-1 crude proteins, with yield 37 and 29 %, respectively. Both enzymes gave single homogenous band of 71 kDa by SDS- PAGE. Also, their optimum pH was 7.0 and they had pH stability from 7.0 – 11.0. The maximum enzyme activities obtained at 55oC and 60°C with Tm (half life temperature) values 86.5 and 83.9ەC for protease and lipase, respectively. The penetration of newly hatched larvae of pink bollworm into the cotton bolls after being dipped in crude or purified protease and lipase each alone or in mixture (v/v) were studied. The results revealed that the penetration percent decreased in pure enzymes than crude. Treatment with the mixed crude enzymes decreased the percentage of penetration than of each enzyme alone. Also, crude lipase , protease and their mixture had repellent action for pink bollworm moths. Moreover, there was highly significant effect on the deformed adult percentage compared with control since the pure enzyme had effective role than crude enzyme. | ||
| Keywords | ||
| Biocontrol; Pectinophora gossypiella; Larval and Pupal mortality percent; Protease and Lipase enzymes; Kinetic properties | ||
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