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1.
J Appl Microbiol ; 125(3): 632-645, 2018 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-29786939

RESUMEN

Alternative energy sources have received increasing attention in recent years. The possibility of adding value to agricultural wastes, by producing biofuels and other products with economic value from lignocellulosic biomass by enzymatic hydrolysis, has been widely explored. Lignocellulosic biomass, as well as being an abundant residue, is a complex recalcitrant structure that requires a consortium of enzymes for its complete degradation. Pools of enzymes with different specificities acting together usually produce an increase in hydrolysis yield. Enzymatic cocktails have been widely studied due to their potential industrial application for the bioconversion of lignocellulosic biomass. This review presents an overview of enzymes required to degrade the plant cell wall, paying particular attention to the latest advances in enzymatic cocktail production and the main results obtained with cocktails used to degrade a variety of types of biomass, as well as some future perspectives within this field.


Asunto(s)
Biocombustibles , Biomasa , Celulasas/metabolismo , Lignina/metabolismo , Hidrólisis
2.
J Appl Microbiol ; 124(5): 1122-1130, 2018 May.
Artículo en Inglés | MEDLINE | ID: mdl-29159986

RESUMEN

AIMS: A new L-asparaginase produced by Streptomyces ansochromogenes UFPEDA 3420 actinobacteria was used in this study against human lymphocyte cultures to evaluate the immunological profile induced by this enzyme. METHODS AND RESULTS: Cultures of lymphocytes were stimulated with S. ansochromogenes L-asparaginase, and cytotoxicity, cell viability, cell stimulation and cytokine production were analysed. This new S. ansochromogenes L-asparaginase induced activation and proliferation of the TCD8+ lymphocyte subset and produced higher TNF-α, IFN-γ, IL-2 and IL-10 levels in a 24-h assay. CONCLUSION: Streptomyces ansochromogenes L-asparaginase is a promising molecule to be used in in vivo models and to deepen preclinical tests against acute lymphoblast leukaemia. SIGNIFICANCE AND IMPACT OF STUDY: L-asparaginase is an indispensable component of the chemotherapeutic treatment of acute lymphoblast leukaemia (ALL) and acute myeloid leukaemia (AML). Currently, drugs such as Asparaginase® , Kidrolase® , and Elspar® and Erwinase® are efficient against leukemic disease, but promote immunosuppression and other side effects in human organisms. Our purified S. ansochromogenes L-asparaginase showed promissory results inducing, in vitro, higher immunostimulation in human PBMC, especially in T CD8+ lymphocyte subsets.


Asunto(s)
Asparaginasa/farmacología , Linfocitos T CD8-positivos/efectos de los fármacos , Activación de Linfocitos/efectos de los fármacos , Streptomyces/enzimología , Células TH1/efectos de los fármacos , Asparaginasa/aislamiento & purificación , Asparaginasa/toxicidad , Linfocitos T CD8-positivos/inmunología , Humanos , Leucocitos Mononucleares/efectos de los fármacos , Leucocitos Mononucleares/inmunología
3.
Appl Microbiol Biotechnol ; 100(12): 5205-14, 2016 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-27112349

RESUMEN

Hemicelluloses are a vast group of complex, non-cellulosic heteropolysaccharides that are classified according to the principal monosaccharides present in its structure. Xylan is the most abundant hemicellulose found in lignocellulosic biomass. In the current trend of a more effective utilization of lignocellulosic biomass and developments of environmentally friendly industrial processes, increasing research activities have been directed to a practical application of the xylan component of plants and plant residues as biopolymer resources. A variety of enzymes, including main- and side-chain acting enzymes, are responsible for xylan breakdown. Xylanase is a main-chain enzyme that randomly cleaves the ß-1,4 linkages between the xylopyranosyl residues in xylan backbone. This enzyme presents varying folds, mechanisms of action, substrate specificities, hydrolytic activities, and physicochemical characteristics. This review pays particular attention to different aspects of the mechanisms of action of xylan-degrading enzymes and their contribution to improve the production of bioproducts from plant biomass. Furthermore, the influence of phenolic compounds on xylanase activity is also discussed.


Asunto(s)
Endo-1,4-beta Xilanasas/metabolismo , Xilanos/metabolismo , Xilosidasas/metabolismo , Biomasa , Celulosa/metabolismo , Endo-1,4-beta Xilanasas/química , Glicósido Hidrolasas/química , Glicósido Hidrolasas/metabolismo , Hidrólisis , Fenoles , Plantas/química , Polisacáridos/metabolismo , Especificidad por Sustrato , Xilosidasas/química
4.
Rev. bras. pesqui. méd. biol ; Braz. j. med. biol. res;42(7): 593-598, July 2009. ilus, tab
Artículo en Inglés | LILACS | ID: lil-517801

RESUMEN

Blood and lymphatic vessel proliferation is essential for tumor growth and progression. Most colorectal carcinomas develop from adenomas (adenoma-carcinoma sequence) in a process due to accumulation of molecular genetic alterations. About 5% of adenomatous polyps are expected to become malignant, but data on the differential angiogenic patterns of these lesions in patients with and without concomitant cancer are missing. The aim of the present study is to compare the angiogenic and lymphatic patterns of adenomatous polyps from patients with and without sporadic cancer. Thirty adenomatous polyps (15 from patients with another principal malignant lesion, and 15 from patients without cancer) were submitted to immunohistochemical staining for CD105 (marker for neoangiogenesis) and D2-40 (marker for lymphatic endothelium). Microvessel density and total vascular area were determined by computer image analysis to quantify the immunostained and total areas, and to assess the number of microvessels. Adenomas from patients with carcinoma showed significantly higher values of total vascular area determined by immunostaining for CD105 (cutoff value = 4386 µm²; P = 0.019) and of lymphatic microvessel density determined by immunostaining with D2-40 (cutoff value = 11.5; P = 0.041) when compared with those from patients without cancer. The present data indicate a significant increase in blood microvascular area and in lymphatic microvascular counts in adenomas removed from patients with cancer.


Asunto(s)
Adulto , Anciano , Anciano de 80 o más Años , Femenino , Humanos , Masculino , Persona de Mediana Edad , Pólipos Adenomatosos/patología , Neoplasias Colorrectales/patología , Linfangiogénesis/fisiología , Neovascularización Patológica/patología , Pólipos Adenomatosos/irrigación sanguínea , Pólipos Adenomatosos/química , Anticuerpos Monoclonales/análisis , Antígenos CD/análisis , Biomarcadores/análisis , Neoplasias Colorrectales/irrigación sanguínea , Neoplasias Colorrectales/química , Inmunohistoquímica , Vasos Linfáticos/química , Vasos Linfáticos/patología , Microcirculación , Estudios Retrospectivos , Receptores de Superficie Celular/análisis
5.
Braz J Med Biol Res ; 42(7): 593-8, 2009 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-19466284

RESUMEN

Blood and lymphatic vessel proliferation is essential for tumor growth and progression. Most colorectal carcinomas develop from adenomas (adenoma-carcinoma sequence) in a process due to accumulation of molecular genetic alterations. About 5% of adenomatous polyps are expected to become malignant, but data on the differential angiogenic patterns of these lesions in patients with and without concomitant cancer are missing. The aim of the present study is to compare the angiogenic and lymphatic patterns of adenomatous polyps from patients with and without sporadic cancer. Thirty adenomatous polyps (15 from patients with another principal malignant lesion, and 15 from patients without cancer) were submitted to immunohistochemical staining for CD105 (marker for neoangiogenesis) and D2-40 (marker for lymphatic endothelium). Microvessel density and total vascular area were determined by computer image analysis to quantify the immunostained and total areas, and to assess the number of microvessels. Adenomas from patients with carcinoma showed significantly higher values of total vascular area determined by immunostaining for CD105 (cutoff value = 4386 microm(2); P = 0.019) and of lymphatic microvessel density determined by immunostaining with D2-40 (cutoff value = 11.5; P = 0.041) when compared with those from patients without cancer. The present data indicate a significant increase in blood microvascular area and in lymphatic microvascular counts in adenomas removed from patients with cancer.


Asunto(s)
Pólipos Adenomatosos/patología , Neoplasias Colorrectales/patología , Linfangiogénesis/fisiología , Neovascularización Patológica/patología , Pólipos Adenomatosos/irrigación sanguínea , Pólipos Adenomatosos/química , Adulto , Anciano , Anciano de 80 o más Años , Anticuerpos Monoclonales/análisis , Anticuerpos Monoclonales de Origen Murino , Antígenos CD/análisis , Biomarcadores/análisis , Neoplasias Colorrectales/irrigación sanguínea , Neoplasias Colorrectales/química , Endoglina , Femenino , Humanos , Inmunohistoquímica , Vasos Linfáticos/química , Vasos Linfáticos/patología , Masculino , Microcirculación , Persona de Mediana Edad , Receptores de Superficie Celular/análisis , Estudios Retrospectivos
6.
Genet Mol Res ; 8(1): 284-90, 2009.
Artículo en Inglés | MEDLINE | ID: mdl-19291877

RESUMEN

Human haptoglobin is classified into three major phenotypes: Hp1-1, Hp2-1 and Hp2-2; there are two autosomal alleles Hp*1 and Hp*2, and the Hp*1 allele has two subtypes, Hp*1F and Hp*1S. Haptoglobin acts as an antioxidant, preventing hemoglobin-driven oxidative damage. We used the comet assay to examine oxidative damage to DNA induced by hydrogen peroxide in human leukocytes; we also looked for differences in the antioxidant capacity of haptoglobin subtypes. Haptoglobin genotypes were determined through allele-specific polymerase chain reaction, visualized on a polyacrylamide gel. The Hp1-1 genotype had the least DNA damage; this indicates that Hp alleles differ in their protective effects against oxidative damage. Among Hp*1 alleles, Hp*1F was the most protective.


Asunto(s)
Antioxidantes , Daño del ADN , Haptoglobinas/genética , Peróxido de Hidrógeno/toxicidad , Fenotipo , Adolescente , Adulto , Femenino , Humanos , Leucocitos/efectos de los fármacos , Masculino
7.
Appl Microbiol Biotechnol ; 79(2): 165-78, 2008 May.
Artículo en Inglés | MEDLINE | ID: mdl-18385995

RESUMEN

Hemicellulose is a complex group of heterogeneous polymers and represents one of the major sources of renewable organic matter. Mannan is one of the major constituent groups of hemicellulose in the wall of higher plants. It comprises linear or branched polymers derived from sugars such as D-mannose, D-galactose, and D-glucose. The principal component of softwood hemicellulose is glucomannan. Structural studies revealed that the galactosyl side chain hydrogen interacts to the mannan backbone intramolecularly and provides structural stability. Differences in the distribution of D-galactosyl units along the mannan structure are found in galactomannans from different sources. Acetyl groups were identified and distributed irregularly in glucomannan. Some of the mannosyl units of galactoglucomannan are partially substituted by O-acetyl groups. Some unusual structures are found in the mannan family from seaweed, showing a complex system of sulfated structure. Endohydrolases and exohydrolases are involved in the breakdown of the mannan backbone to oligosaccharides or fermentable sugars. The main-chain mannan-degrading enzymes include beta-mannanase, beta-glucosidase, and beta-mannosidase. Additional enzymes such as acetyl mannan esterase and alpha-galactosidase are required to remove side-chain substituents that are attached at various points on mannan, creating more sites for subsequent enzymatic hydrolysis. Mannan-degrading enzymes have found applications in the pharmaceutical, food, feed, and pulp and paper industries. This review reports the structure of mannans and some biochemical properties and applications of mannan-degrading enzymes.


Asunto(s)
Biotecnología , Mananos/química , Mananos/metabolismo , Manosidasas/metabolismo , Polisacáridos/metabolismo , Manosidasas/química , Polisacáridos/química , Relación Estructura-Actividad , Especificidad por Sustrato
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