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1.
Neotrop Entomol ; 52(2): 283-291, 2023 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-35731370

RESUMO

Spodoptera frugiperda (J.E. Smith) (Lepidoptera: Noctuidae) is an important pest in several regions being the use of Bacillus thuringiensis-based bioproducts an alternative for its control. Firstly, 3 L of an aqueous bioproduct suspension was produced and characterized. Its 50% lethal concentration against molecularly identified corn and rice S. frugiperda strains using an artificial diet were 77.01% (95% CL, 68.16-90.47) and 2.22% (95% CL, 0.01-6.68), respectively. The next objective of this work was to evaluate the performance of this bioproduct in maize against S. frugiperda strains under different simulated agrological regions mimicking their corresponding periodic day/night temperatures. Thus, the impact of environmental temperature on the bioproduct efficacy (E) was studied. It was observed that a warmer scenario (35 °C day/30 °C night) could favor the tolerance of corn S. frugiperda strain to the bioproduct (E = 56.36 ± 0.61%) maintaining a high efficacy (92.44 ± 6.55%) when it was tested against rice S. frugiperda strain. Conversely, under temperate conditions, efficacy values ranged from 84 to 95% for both S. frugiperda strains. On the other hand, based on a foliar feeding damage analysis, our bioproduct displayed a significant foliar protection in maize plants infested with either corn or rice S. frugiperda strains.


Assuntos
Bacillus thuringiensis , Oryza , Animais , Bacillus thuringiensis/genética , Zea mays/genética , Spodoptera/genética , Temperatura , Endotoxinas , Proteínas Hemolisinas/genética , Plantas Geneticamente Modificadas , Proteínas de Bactérias/genética , Larva , Resistência a Inseticidas
2.
Folia Microbiol (Praha) ; 66(6): 1009-1022, 2021 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-34318446

RESUMO

The successfulness of a lipase-catalyzed industrial process depends on a proper lipase selection. In this work, an alternative screening platform for industrially important biotransformations catalyzed by microbial lipases was proposed. Thus, the reactivity of sixty lipase activities from spore-forming microorganisms towards hydrolytic and transesterification reactions by using p-nitrophenyl palmitate as a chromogenic acyl donor substrate was explored. Only three biocatalysts were capable of catalyzing all reactions tested. Fourteen biocatalysts did not show hydrolytic activity at all; however, they displayed transesterification activities using ethanol, starch, low-methoxyl (LM) pectin, high-methoxyl (HM) pectin, or vitamin C as acyl acceptors. Using heat-treated biocatalysts, hydrolytic activities were not highly correlated with the corresponding transesterification activities using ethanol (r = -0.058, p = 0.660), starch (r = 0.431, p = 0.001), LM pectin (r = -0.010, p = 0.938), HM pectin (r = 0.167, p = 0.202), and vitamin C (r = -0.048, p = 0.716) as acyl acceptor. In addition, to the best of our knowledge, several transesterification activities produced from microorganisms of the genus Bacillus, Brevibacillus, Lysinibacillus, Geobacillus, or Sporosarcina were reported for first time. Finally, the global lipase market was presented and segmented by date, application, geography and player highlighting the commercial contribution of microbial lipases.


Assuntos
Lipase , Biotransformação , Catálise , Esterificação , Hidrólise , Lipase/metabolismo
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