Single cell protein production by Candida robusta isolated from sugar cane (Saccharum sp.) for animal feed / Produção de Biomassa por Candida robusta isolada da Cana-de-açúcar (Saccharum sp.) para alimentação animal

The protein obtained from the microorganisms is not only cheap but can be used as additive to provide a balanced nutrition for many animals feeding. The aim of this work was the single cell protein (SCP) production by Candida robusta URM5293 using sugarcane bagasse as substrate. The yeast C. robusta URM5293 was isolated from root sugarcane and was identified based on morphological and biochemical characteristics. Biomass production was done into Erlenmayers flasks (250 mL) containing culture medium supplemented of sugarcane bagasse hydrolyzate. Fermentations were carried varying culture conditions through the study of four different variables: temperature (25, 30, and 35°C), agitation intensity (110, 140 or 170 rpm), pH (6.0, 7.0, and 8.0) and production time (72, 96, and 120h), according to a 24-1 fractional factorial design. Results demonstrated that this yeast was able to ensure the highest level of biomass (141 g/L) when cultivated at 25°C, pH 6.0, 170 rpm of agitation intensity after 72h of cultivation using sugarcane bagasse. The present results demonstrate the potential of sugarcane bagasse hemicellulosic hydrolyzate as a substrate for the production of microbial protein by C. robusta URM5293

Single cell protein production by Candida robusta isolated from sugar cane (Saccharum sp.) for animal feed: Produção de Biomassa por Candida robusta isolada da Cana-de-açúcar (Saccharum sp.) para alimentação animal

The protein obtained from the microorganisms is not only cheap but can be used as additive to provide a balanced nutrition for many animals feeding. The aim of this work was the single cell protein (SCP) production by Candida robusta URM5293 using sugarcane bagasse as substrate. The yeast C. robusta URM5293 was isolated from root sugarcane and was identified based on morphological and biochemical characteristics. Biomass production was done into Erlenmayers flasks (250 mL) containing culture medium supplemented of sugarcane bagasse hydrolyzate. Fermentations were carried varying culture conditions through the study of four different variables: temperature (25, 30, and 35°C), agitation intensity (110, 140 or 170 rpm), pH (6.0, 7.0, and 8.0) and production time (72, 96, and 120h), according to a 24-1 fractional factorial design. Results demonstrated that this yeast was able to ensure the highest level of biomass (141 g/L) when cultivated at 25°C, pH 6.0, 170 rpm of agitation intensity after 72h of cultivation using sugarcane bagasse. The present results demonstrate the potential of sugarcane bagasse hemicellulosic hydrolyzate as a substrate for the production of microbial protein by C. robusta URM5293

Purification of a lectin from Cratylia mollis crude extract seed by a single step PEG/phosphate aqueous two-phase system

The partitioning and purification of lectins from the crude extract of Cratylia mollis seeds (Cramoll 1,4) was investigated in aqueous two-phase systems (ATPS). A factorial design model (24) was used to evaluate the influence of polyethylene glycol (PEG) molar mass (15008000g/mol), PEG concentration (12.517.5% w/w), phosphate (1015% w/w) concentration, and pH (68) on the differential partitioning, purification factor, and yield of the lectin. Polymer and salt concentration were the most important variables affecting partition of lectin and used to find optimum purification factor by experimental BoxBehnken design together with the response surface methodology (RSM). ATPS showed best conditions composed by 13.9% PEG1500, 15.3% phosphate buffer at pH 6, which ensured purification factor of 4.70. Sodium dodecyl sulfatepolyacrylamide gel electrophoresis showed a single band of protein with 26.1kDa. Furthermore, results demonstrated a thermostable lectin presenting activity until 60°C and lost hemagglutinating activity at 80°C. According to the obtained data it can be inferred that the ATPS optimization using RSM approach can be applied for recovery and purification of lectins.We are grateful to the following bodies for the grants awarded: CAPES (Coordination for the Improvement of Level Personnel Superior); FACEPE (Pernambuco Science and Technology Foundation): Researcher's scholarship grant: BFP-0017-5.05/18 CNPq (National Council for Scientific Development and Technological) process: 427153/2016-6 and we also thank the reviewers for their valuable comments and suggestions as these helped us to improve the manuscript.info:eu-repo/semantics/publishedVersio

Potential of quixaba (Sideroxylon obtusifolium) latex as a milk-clotting agent

There are several obstacles to the use of chymosin in cheese production. Consequently, plant proteases have been studied as possible rennet substitutes, but most of these enzymes are unsuitable for the manufacture of cheese. The aim of this study was to evaluate the potential of latex from Sideroxylon obtusifolium as a source of milk-clotting proteases and to partially characterize the enzyme. The enzyme extract showed high protease and coagulant activities, with an optimal pH of 8.0 and temperature of 55 °C. The enzyme was stable in wide ranges of temperature and pH. Its activity was not affected by any metal ions tested; but was inhibited by phenylmethanesulfonyl fluoride and pepstatin. For the coagulant activity, the optimal concentration of CaCl2 was 10 µmol L- 1. Polyacrylamide gel electrophoresis showed four bands, with molecular weights between 17 and 64 kDa. These results indicate that the enzyme can be applied to the cheese industry

Potencial do latex da fruta pão (Artocarpus altilis) como agente coagulante do leite

A fruta-pão é uma árvore exótica no Brasil, onde se aclimatou muito bem. Embora seja uma planta lactífera, o conhecimento sobre seu látex é escasso. No entanto, sabe-se que enzimas proteolíticas correspondem a mais de 50% da composição do látex em plantas lactíferas. O objetivo deste estudo foi avaliar o potencial do látex da fruta-pão (Artocarpus altilis var. Apyrena) como fonte de protease coagulante do leite e caracterizar parcialmente a enzima. A atividade proteolítica da fração de extrato bruto foi avaliada utilizando azocaseína e, para a quantificação das proteínas totais, o ácido bicinconínico (BCA). A atividade de coagulação do leite foi testada utilizando leite desnatado a 12%. A protease foi testada em diferentes condições de temperatura (35 a 80°C) e pH (5,8 a 10,7) e apresentou atividade ótima a 50°C e pH alcalino (8,5) sendo estável a estas variáveis durante 120 minutos. A atividade coagulante no leite foi diretamente proporcional à temperatura na melhor concentração de CaCl2 a 10µmol L-1. Os resultados indicam que a enzima analisada é uma possível alternativa à quimosin