Rodrigo Simões Ribeiro Leite

ORCID: 0000-0002-0837-5072
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About
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Research Areas
  • Enzyme Production and Characterization
  • Biofuel production and bioconversion
  • Enzyme Catalysis and Immobilization
  • Polysaccharides and Plant Cell Walls
  • Microbial Metabolites in Food Biotechnology
  • Fermentation and Sensory Analysis
  • Phytase and its Applications
  • Polysaccharides Composition and Applications
  • Fungal Biology and Applications
  • Protein Hydrolysis and Bioactive Peptides
  • Fungal and yeast genetics research
  • Microbial Metabolism and Applications
  • Phytochemicals and Antioxidant Activities
  • Food composition and properties
  • Plant tissue culture and regeneration
  • Ruminant Nutrition and Digestive Physiology
  • Enzyme-mediated dye degradation
  • Mycotoxins in Agriculture and Food
  • Pineapple and bromelain studies
  • Biochemical and biochemical processes
  • Agricultural and Food Sciences
  • Meat and Animal Product Quality
  • Chemical synthesis and alkaloids
  • Cassava research and cyanide
  • Studies on Chitinases and Chitosanases

Universidade Federal da Grande Dourados
2015-2024

Discovery Air (Canada)
2024

Universidade Estadual Paulista (Unesp)
2007-2011

β-Glucosidases catalyze the hydrolysis of cellobiose and cellodextrins, releasing glucose as main product. This enzyme is used in food, pharmaceutical, biofuel industries. The aim this work to improve β-glucosidase production by fungus Lichtheimia ramosa solid-state fermentation (SSF) using various agroindustrial residues evaluate catalytic properties enzyme. A high β-glucosidase, about 274 U/g dry substrate (or 27.4 U/mL), was obtained cultivating on wheat bran with 65% initial moisture, at...

10.1016/j.ejbt.2015.05.007 article EN cc-by Electronic Journal of Biotechnology 2015-06-30

For the first time, production of an extracellular β-glucosidase (Sp-β-gl) by a Sporidiobolus pararoseus yeast strain is reported. The Sp-β-gl activity was quantified, characterized, and assessed for its efficiency in releasing aroma-enhancing compounds wines. maximum enzymatic synthesis after 72 h growth complex media with 20 g/L cellobiose. optimal pH temperature were 5.5 at 50 °C, respectively. It showed wide range stability exhibited quite high thermostability low temperatures. In...

10.1111/j.1750-3841.2011.02293.x article EN Journal of Food Science 2011-08-05

Microbial β-glucosidases can be used in several industrial processes, including production of biofuels, functional foods, juices, and beverages. In the present work, β-glucosidase by solid state cultivation fungus Thermoascus crustaceus a low-cost medium (comprising agroindustrial residues) was evaluated. The highest β-glucosidase, about 415.1 U/g substrate (or 41.51 U/mL), obtained cultivating wheat bran with 70% humidity, during 96 h at 40°C. enzymatic activity optimum pH 4.5 65°C....

10.1590/0001-3765202120191349 article EN cc-by Anais da Academia Brasileira de Ciências 2021-01-01

Background: Enzyme production by solid state bioprocess (SSB) using residues as substrate for microorganisms is an alternative costs reduction and to avoid their disposal into environment.The aim of this work was evaluate the physiology fungus Lichtheimia ramosa in terms microbial growth amylases, β-glucosidases, carboxymethylcellulase (CMCase), xylanases, via SSB, utilizing wastes Brazilian savannah fruits bocaiuva (Acrocomia aculeata), guavira (Campomanesia pubescens) pequi (Caryocar...

10.2225/vol16-issue5-fulltext-7 article EN cc-by-nc-nd Electronic Journal of Biotechnology 2013-09-15

Invertases are used for several purposes; one among these is the production of fructooligosaccharides. The aim this study was to biochemically characterize invertase from industrial Saccharomyces cerevisiae CAT-1 and Rhodotorula mucilaginosa isolated Cerrado soil. optimum pH temperature were 4.0 70 °C 4.5 50 invertase. thermal stability 3.0 10.5 75 R. invertase, respectively. S. 7.0, °C, Both enzymes showed good catalytic activity with 10% ethanol in reaction mixture. hydrolysis by...

10.1080/10826068.2018.1466155 article EN Preparative Biochemistry & Biotechnology 2018-06-22

Among the enzymes of cellulolytic complex, β-glucosidases are noteworthy due to possibility their application in different industrial processes, such as production biofuels, winemaking, and development functional foods. This study aimed evaluate characterization β-glucosidase from filamentous fungus Gongronella butleri, recently isolated Cerrado soil cultivated agro-industrial residue substrates. The highest β-glucosidase, about 215.4 U/g dry substrate (or 21.5 U/mL), was obtained by...

10.5897/ajb2015.15025 article EN cc-by AFRICAN JOURNAL OF BIOTECHNOLOGY 2016-04-20

Protease production was carried out in solid state fermentation. The enzyme purified through precipitation with ethanol at 72% followed by chromatographies columns of Sephadex G75 and Sephacryl S100. It 80-fold exhibited recovery total activity 0.4%. SDS-PAGE analysis indicated an estimated molecular mass 24.5 kDa the N-terminal sequence first 22 residues APYSGYQCSMQLCLTCALMNCA. Purified protease only inhibited EDTA (96.7%) stimulated Fe(2+) revealing to be a metalloprotease activated iron....

10.1021/jf9017977 article EN Journal of Agricultural and Food Chemistry 2009-09-11

An exo-PG obtained from Penicillium viridicatum in submerged fermentation was purified to homogeneity. The apparent molecular weight of the enzyme 92 kDa, optimum pH and temperature for activity were 5 50-55 degrees C. showed a profile an exo-polygalacturonase, releasing galacturonic acid by hydrolysis pectin with high degree esterification (D.E.). Ions Ca(2+) enhanced stability its 30%. K(m) 1.30 absence 1.16 mg mL(-1) presence this ion. In relation V(max) ion increased 1.76 2.07 mumol...

10.1155/2009/631942 article EN cc-by International Journal of Microbiology 2009-01-01

Polygalacturonases are enzymes involved in the degradation of pectic substances, being extensively used food industries, textile processing, degumming plant rough fibres, and treatment wastewaters. Polygalacturonase (PG) production by thermophilic fungus Thermoascus aurantiacus on solid-state fermentation was carried out culture media containing sugar cane bagasse orange proportions 30% 70% (w/w) at 45°C for 4 days. PG obtained purified gel filtration ion-exchange chromatography. The highest...

10.1155/2013/438645 article EN Enzyme Research 2013-09-12

Peptidases are important because they play a central role in pharmaceutical, food, environmental, and other industrial processes. A serine peptidase from Aspergillus terreus was isolated after two chromatography steps that showed yield of 15.5%. Its molecular mass determined to be 43 kD, by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). This active between pH 5.0 8.0 had maximum activity at 7.0, 45°C. When exposited with 1 M urea, the enzyme maintained 100% used...

10.1080/10826068.2015.1031387 article EN Preparative Biochemistry & Biotechnology 2015-04-01

Profiling microorganisms with potential for amylase production in low cost culture media has been widely recognized due to its broad applicability. The aim of this study was select yeast strains produce amylolytic enzymes by solid state fermentation. Fifty-four (54) were assessed and three exhibited ability amylases: Candida parapsilosis 14.68 U/mL (146.8 U/g substrate); Rhodotorula mucilaginosa 25.0 (250 substrate), glabrata 25.39 (253.9 fermentation, 120 h at 28°C, using wheat bran 70%...

10.5897/ajb2014.14062 article EN cc-by AFRICAN JOURNAL OF BIOTECHNOLOGY 2015-04-08

The present study compared the production and catalytic properties of amylolytic enzymes obtained from fungi Lichtheimia ramosa (mesophilic) Thermoascus aurantiacus (thermophilic). highest amylase in both was observed wheat bran supplemented with nutrient solution (pH 4.0) after 96 hours cultivation, reaching 417.2 U/g dry substrate (or 41.72 U/mL) 144.5 14.45 for L. T. , respectively. showed higher activity at pH 6.0 60°C. amylases produced by were stable between 3.5–10.5 4.5–9.5, 55°C 1...

10.1155/2016/7323875 article EN cc-by The Scientific World JOURNAL 2016-01-01
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