Caracterização da fração protéica da cianobactéria Aphanothece Microscopica Nägeli cultivada no efluente da parboilização do arroz

Abstract

RESUMOO objetivo do presente trabalho foi avaliar a fração protéica da cianobactéria Aphanothece microscopica Nägeli cultivada no efluente da parboilização do arroz quando submetida a diferentes condições de secagem. A produção da biomassa foi realizada a partir da água residuária do processo de parboilização do arroz em bioreatores de coluna de bolhas. A biomassa foi separada do efluente por centrifugação e desidratada em secador descontínuo de bandejas nas condições de 40, 50 e 60ºC e espessuras de bandejas de 5 e 7 mm. O comportamento eletroforético das proteínas da biomassa foi analisado por eletroforese em gel de poliacrilamamida na presença de dodecil sulfato de sódio (SDS-PAGE) e apresentou bandas com peso molecular de 15 kDa a 62,5 kDa. O perfil aminoacídico mostrou teores superiores aos recomendados pelo padrão FAO, com exceção dos aminoácidos lisina e dos sulfurados (MET+CYS). A caracterização funcional, expressa em termos de solubilidade e capacidade emulsificante, demonstrou a influência da condição de secagem na funcionalidade protéica da biomassa. Palavras chave: cianobactéria, Aphanothece microscopica Nägeli, proteína, aminoácidos. SUMMARYPROTEIN CHARACTERISATION OF THE Aphanothece microscopica Nägeli CYANOBACTERIUM CULTIVATED IN PARBOILED RICE EFFLUENT. The objective of the present work was to evaluate the protein fraction of Aphanothece microscopica Nägeli cyanobacteria cultivated in the parboiled rice effluent, submitted to different drying conditions. The production of the biomass was done by using wastewater from the process of rice parboiling in a bubble column bioreactor. The biomass was separated from the effluent by centrifugation and dehydrated in a tray dryer at 40, 50 and 60 o C and thicknesses of 5 and 7 mm. The eletroforetic profile of proteins of the biomass was analysed by SDS-PAGE and presented bands with molecular weight between 62.5-15kDa. The amino acid profile was higher than the concentrations recommended by standard FAO, with the exception of the amino acids (LYS) and the sulphurated (MET+CYS). The functional properties characterisation in terms of protein solubility and emulsification capacity demonstrated the influence of the drying condition in the protein functionality of the biomass.

Sustainable Approaches for ‘Protein Accessibility

“…The term Single cell protein refers to the purified proteins isolated from the microorganisms and / or the bulk of dried cells of microorganisms like bacteria, algae, yeast and fungi with high protein content. They are rich in proteins with various essential amino acids (lysine and me-INGLE S377 thionine) and vitamins (Jacob-Lopes et al, 2006).…”

Substituting Fish Meal with a Bacteria Protein (Clostridium autoethanogenum Protein) Derived from Industrial-Scale Gas Fermentation: Effects on Growth and Gut Health of Juvenile Large Yellow Croakers (Larimichthys crocea)

“…Single-cell proteins are cellular manufactured products of microorganisms such as yeast, bacteria, actinomycetes, molds, microalgae and higher fungi produced in the largescale factory [7]. Single-cell protein powder is a cytoplasmic mass mixture of proteins, carbohydrates, fats, nucleic acids, vitamins and inorganic substances [8], which is an important source of protein for the food and feed industries [9]. Clostridium autoethanogenum is regarded as a naturally occurring non-pathogenic strain and can use carbon monoxide as its carbon and energy source and for industrial-scale gas fermentation [10].…”

Heterotrophic growth of Aphanothece microscopica Nägeli in calcium alginate beads from BG11 medium and vinasse

“…Chorococcaceae that forms blue-green colonies (approximately 9.0 -9.5 µm by 4.0 -4.2 µm), that has been studied for wastewater treatment, valorization of residues, single-cell protein and phycocyanin production (JACOB-LOPES et al, 2006;JACOB-LOPES et al, 2007;LACERDA;FRANCO, 2008;ZEPKA et al, 2010;BASTOS et al, 2014;MORAIS;BASTOS, 2018).…”