Purification and characterization of an extracellular keratinolytic protease from a new isolate of Aspergillus parasiticus

INTRODUÇÃOO pirarucu (Arapaima gigas), conhecido popularmente como Gigante da Amazônia, tem vasta distribuição na Bacia Amazônica, sendo o maior peixe dulcícola de escama do mundo. Na Região ABSTRACT RESUMOAmazônica, seu consumo é um hábito tradicional, que tem se expandido para outras regiões, devido ao sabor de sua carne, valor nutritivo e também comercial (Mueller & Green 2006, FAO 2010 O beneficiamento do pirarucu (Arapaima gigas) gera grande quantidade de resíduos que podem ser aproveitados para a elaboração de novos produtos de interesse industrial. Este estudo objetivou avaliar a produção de hidrolisados proteicos a partir de resíduos de pirarucu, utilizando-se proteases de Aspergillus flavo-furcatis e pancreatina comercial, além de caracterizá-los quanto às suas qualidades nutricional e microbiológica. A matéria-prima utilizada foi carne mecanicamente separada de carcaças de pirarucu (CMSP). Dois produtos foram desenvolvidos: um hidrolisado proteico de pirarucu produzido com enzima comercial (HPPEC) e outro com enzima microbiana (HPPEM). A CMSP e os hidrolisados foram submetidos à análise de composição química, qualidade microbiológica, grau de hidrólise, digestibilidade e perfil de aminoácidos. Os resultados mostraram que, no HPPEC, o teor proteico foi de 73,47 %, significativamente superior ao do HPPEM (58,03 %). Todavia, os dois produtos apresentaram altos valores de digestibilidade, ausência de contaminantes microbianos e redução no conteúdo de lipídios. Entre as enzimas utilizadas, a pancreatina foi a mais eficiente na elaboração do produto final, que demonstrou conteúdo de aminoácidos essenciais superior aos requerimentos para humanos adultos. O hidrolisado desenvolvido com as enzimas de A. flavo-furcatis apresentou escore de aminoácidos essenciais inferior a 1,0, sendo o aminoácido mais limitante o triptofano. PALAVRAS-CHAVE:Aspergillus sp.; aproveitamento de resíduos; coprodutos de pescado. Production of arapaima protein hydrolysate using Aspergillus flavo-furcatis protease and pancreatinThe processing of arapaima (Arapaima gigas) generates a lot of residues that can be used for the development of new products of industrial interest. This study aimed at evaluating the production of protein hydrolysates from arapaima residues using Aspergillus flavo-furcatis protease and commercial pancreatin, as well as characterizing their nutritional and microbiological qualities. The raw material used was meat mechanically separated from arapaima carcasses (MMSA). Two products were developed: a protein hydrolysate of arapaima using a commercial enzyme (PHACE) and another one using microbial enzyme (PHAME). The MMSA and the hydrolysates were analyzed for chemical composition, microbiological quality, degree of hydrolysis, digestibility and amino acid profile. The results showed that the PHACE protein content was 73.47 %. This value was significantly higher, when compared to the PHAME (58.03 %). However, both products showed high digestibility values, absence of microbial contaminants and reduced lipid content. ...

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“…The characterization of proteases from Aspergillus tamarii was established according to similar characteristics of this enzyme compared to other proteases. Aspergillus tamarii NA 9.0 Serine protease [26] Aspergillus parasiticus 50˚C 7.0 Serine protease [44] Aspergillus flavus 45˚C 7.5 Serine protease [40] Aspergillus niger NA 9.0 Metalloproteases [45] Aspergillus niger 60˚C 8.0 Metalloproteases [46] Aspergillus niger 40˚C 3.5 Aspartic protease [47] Aspergillus carbonarius 40˚C 3.0 Cysteine protease [48] NA = Not Available. and Azocasein (ZA), using both substrates a hydrolyzed band appeared as a white band that corresponded to the position of the protease in the gel.…”

Section: Effect Of Inhibitors On Proteolytic Activitymentioning

confidence: 99%

Novel Protease from <i>Aspergillus tamarii</i> URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation

Silva¹,

Oliveira²,

Souza-Motta³

et al. 2016

AER

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This study reports the protease production from Aspergillus tamarii using agroindustrial residues as substrate for solid-state fermentation (SSF) and biochemical characterization. The highest protease production was obtained using wheat bran as substrate at 72 h fermentation with maximum proteolytic activity of 401.42 U/mL, collagenase of 243.0 U/mL and keratinase of 19.1 U/mL. The protease exhibited K M = 18.7 mg/mL and Vmax = 28.5 mg/mL/min. The optimal pH was 8.0 and stable in a wide pH range (5.0 -11.0) during 24 h. The optimum temperature was 40˚C. The proteolytic activity was inhibited by Cu 2+ (33.98%) and Hg 2+ (22.69%). The enzyme was also inhibited by PMSF (65.11%), indicating that is a Serine Protease. These properties suggest that alkaline protease from A. tamarii URM4634 is suitable for application in food industries and leather processing. Additionally, the present findings opened new vistas in the utilization of wheat bran and other effective agroindustrial wastes as substrates for SSF.

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Purification and characterization of an extracellular keratinolytic protease from a new isolate of Aspergillus parasiticus

Cited by 108 publications

References 35 publications

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

Produção de hidrolisado proteico de pirarucu utilizando-se protease de Aspergillus flavo-furcatis e pancreatina

Novel Protease from <i>Aspergillus tamarii</i> URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation

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Purification and characterization of an extracellular keratinolytic protease from a new isolate of Aspergillus parasiticus

Cited by 108 publications

References 35 publications

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

A novel organic solvent- and detergent-stable serine alkaline protease from Trametes cingulata strain CTM10101

Produção de hidrolisado proteico de pirarucu utilizando-se protease de Aspergillus flavo-furcatis e pancreatina

Novel Protease from &lt;i&gt;Aspergillus tamarii&lt;/i&gt; URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation

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Novel Protease from <i>Aspergillus tamarii</i> URM4634: Production and Characterization Using Inexpensive Agroindustrial Substrates by Solid-State Fermentation