The digestive apparatus of termites may have several biotechnological applications, as well as being a target for pest control. This report discusses the detection of cellulases (endoglucanase, exoglucanase, and β-glucosidase), hemicellulases (β-xylosidase, α-l-arabinofuranosidase, and β-d-xylanase), α-amylase, and proteases (trypsin-like, chymotrypsin-like, and keratinase-type) in gut extracts from Nasutitermes corniger workers and soldiers. Additionally, the effects of pH (3.0-11.0) and temperature (30-100°C) on enzyme activities were evaluated. All enzymes investigated were detected in the gut extracts of worker and soldier termites. Endoglucanase and β-xylanase were the main cellulase and hemicellulase, respectively. Zymography for proteases of worker extracts revealed polypeptides of 22, 30, and 43kDa that hydrolyzed casein, and assays using protease inhibitors showed that serine proteases were the main proteases in worker and soldier guts. The determined enzyme activities and their response to different pH and temperature values revealed that workers and soldiers contained a distinct digestive apparatus. The ability of these termites to efficiently digest the main components of lignocellulosic materials stimulates the purification of gut enzymes. Further investigation into their biotechnological potential as well as whether the enzymes detected are produced by the termites or by their symbionts is needed.
Aims: This work aimed to isolate, characterize and evaluate the antimicrobial activity of a trypsin inhibitor (PgTI) from the stem of Pilosocereus gounellei. Place and Duration of Study: Methodology: PgTI was isolated from P. gounellei stem extract by gel filtration and ion exchange chromatographies. The inhibitor was characterized by isoelectric focusing, polyacrylamide gel electrophoresis, tryptic digestion followed by mass spectrometry analysis and for stability towards heating. Antibacterial and antifungal activities were investigated through broth microdilution assays. Viability of the microbial cells was also evaluated by flow cytometry analysis using thiazol orange and propidium iodide. Results: PgTI appeared as a single polypeptide band of 37.1 kDa and isoelectric point (pI) 5.88. The inhibition constant (K i ) for bovine trypsin was 14 nM and mass spectrometry analysis of PgTI did not reveal similarities with other plant proteins. Trypsin inhibitor activity was stable at temperatures up to 50ºC. PgTI inhibited growth of Gram-positive and Gram-negative bacteria (minimal inhibitory concentrations (MIC) from 7.5 to150 µg/mL) with bactericidal activity only against Escherichia coli (minimal bactericidal concentration: 75.0 µg/mL). PgTI also inhibited the growth of Candida krusei (MIC of 60 µg/mL). Flow cytometry confirmed that PgTI did not affect the viability of E. coli and C. krusei cells at the MIC. Conclusion: This is the first report on a bioactive protein purified from P. gounellei, which provides biotechnological value to this cactus.
As lectinas são um grupo de proteínas que possuem como característica principal a capacidade de estabelecer interações específica e reversivelmente a carboidratos. O objetivo deste trabalho foi realizar um levantamento bibliográfico acerca das atividades biotecnológicas das lectinas da espécie Bauhinia forficata, tradicionalmente utilizada na medicina popular por suas propriedades hipoglicemiantes, inclusive é uma das espécies listadas como de interesse ao SUS. Foi realizada busca por artigos científicos no Google Acadêmico, estabelecendo-se como recorte temporal o período de 2000 a 2020. Alguns descritores foram estabelecidos, e os artigos foram escolhidos conforme a relevância. Duas lectinas de B. forficata foram purificadas e caracterizadas, e há trabalhos que relatam estudos com proteínas recombinantes devido à dificuldade de se trabalhar com a forma natural. Dentre as potencialidades biotecnológicas para B. forficata está sua ação anticâncer, tendo sido registrada sua eficácia contra várias linhagens de células cancerígenas, como melanoma, câncer de mama e colorretal.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.
customersupport@researchsolutions.com
10624 S. Eastern Ave., Ste. A-614
Henderson, NV 89052, USA
Copyright © 2024 scite LLC. All rights reserved.
Made with 💙 for researchers
Part of the Research Solutions Family.