Abstract The global food loss and waste is the most urgent research area in food science to attend the current demand for more sustainable and profitable processes. Along the productive chain about 1/3 of the food is lost or wasted, this number reaches 1/2 for fruit and vegetable production in developing countries. Brazil has been investing in researches aiming to turn its wastes into byproducts, as biomolecules of high value such as lipases. These enzymes are found in a high diversity of plant sources and their researches are covered by promising market growth expectations due to the current demand for biofuels and bio-transformed food. Thus, the aim of the present study is to discuss the potential of wastes generated by the Brazilian fruit processing to become a source of lipases, by the analysis of the most recent studies on fruit lipases, as well as the inclusion of this process in the biorefinery concept. According to this concept, different products can be obtained from the same raw material. Considering the confirmation of the presence of lipases on fruit wastes, the annual fruit production and the percentage of residues, the assessed data showed that wastes from the processing of orange, mango, papaya and palmare promising for lipase obtainment.

O presente estudo visou a produção, purificação e aplicação da quitinase extracelular da linhagem Cellulosimicrobium cellulans 191. A maior produção de quitinase em frascos agitados foi 6,9 U/mL após 72 h de fermentação a 25ºC e 200 rpm. Em fermentador de 5 L utilizando aeração de 1,5 vvm, a maior atividade da enzima foi 4,19 U/mL após 168 h de fermentação a 25ºC e 200 rpm; e com 3 vvm, foi obtido 4,38 U/mL após 144 h de fermentação. A quitinase (61 KDa) foi purificada cerca de 6,65 vezes em coluna de filtração em gel Sepharose CL 4B 200 com um rendimento de 46,61%. A enzima purificada foi capaz de lisar a parede celular de alguns fungos e formar protoplastos.

This study concerned the production, purification and application of extracellular chitinase from Cellulosimicrobium cellulans strain 191. In shaken flasks the maximum yield of chitinase was 6.9 U/mL after 72 h of cultivation at 25ºC and 200 rpm. In a 5 L fermenter with 1.5 vvm aeration, the highest yield obtained was 4.19 U/mL after 168 h of fermentation at 25ºC and 200 rpm, and using 3 vvm, it was 4.38 U/mL after 144 h of fermentation. The chitinase (61 KDa) was purified about 6.65 times by Sepharose CL 4B 200 gel filtration with a yield of 46.61%. The purified enzyme was able to lyse the cell walls of some fungi and to form protoplasts.

O presente trabalho visou a aplicação da enzima quitinolítica purificada da linhagem Cellulosimicrobium cellulans 191 e da preparação comercial de papaína na hidrólise da quitina coloidal. A quitina coloidal foi caracterizada quanto ao grau de desacetilação e apresentou GD de 14% por espectroscopia na região do infravermelho. A quitinase purificada hidrolisou a quitina coloidal liberando di-N-acetilquitobiose, enquanto que a preparação comercial de papaína atuando sobre o mesmo substrato formou di-N-acetilquitobiose e tri-N-acetilquitotriose. A estrutura química dos aminoglucanooligossacarídeos foi elucidada por espectrometria de massa.

The aim of this work was the application of purified chitinolytic enzyme from Cellulosimicrobium cellulans 191 and the commercial papain in the hydrolysis of colloidal chitin. The latter was characterized with regard to the degree deacetylation (GD), with a GD of 14% being obtained using infrared spectroscopy. The purified chitinase hydrolysed the colloidal chitin and formed di-N-acetylchitobiose, while the commercial papain acting on the same substrate formed di-N-acetylchitobiose and tri-N-acetylchitotriose. The aminoglucanoligosaccharides chemical structure was elucidated by mass spectrometry.