RESUMO -O objetivo do presente trabalho foi a obtenção das curvas de secagem, o ajuste do modelo da difusão líquida e a determinação dos coeficientes de difusão de folhas da casca e polpa da fruta abricó (Mammea americana), submetidas a diferentes temperaturas do ar de secagem. Para uma eventual comparação dos resultados, realizaram-se os tratamentos de secagem com três níveis de temperatura do ar de secagem (40, 50 e 60°C). Os valores da difusividade efetiva obtidos variaram 1,20 x 10 -04 a 5,95 x 10 -04 mm 2 s -1 e 1,40 x 10 -04 a 3,50 x 10 -04 mm 2 s -1 para a casca e polpa do abricó, respectivamente. A difusividade aumentou com o aumento da temperatura do ar de secagem e a energia de ativação para a difusão líquida variou de 3,061 KJ mol -1 para a casca do abricó e 3,979 KJ mol -1 para a polpa do mesmo além de erros relativos médios abaixo de 0,1. INTRODUÇÃODe nome científico Mammea americana, o abricó também pode ser conhecido como abricó-do-pará, abricote e abricoteiro. Seu fruto é carnoso, possui somente uma semente, é duro e redondo. É consumido principalmente nos Estados Unidos, e no Brasil, é mais consumido no estado do Pará. A árvore é frondosa, grande e piramidal e pode chegar aos 15 metros de altura. As folhas podem medir até 14 cm de comprimento, e são pecioladas. As flores são brancas, perfumadas e aparecem solitárias ou em pares opostos (PETRIN, 2016).Por se tratar de uma fruta ainda silvestre a colheita ainda tem caráter extrativista, e, depois da coleta os frutos são repassados para intermediários a um baixo custo e revendidos em mercados maiores a um valor mais elevado. No atual cenário, a demanda é pequena e destinada apenas aos consumidores locais (BRAGA et al., 2010). Apesar de o congelamento ser o método mais clássico de conservação da polpa, o acondicionamento pela secagem também pode ser considerado por se basear no fato de que tanto os microrganismos como as enzimas e todo o mecanismo metabólico necessitam de certa quantidade de água para suas atividades. Com a redução da água disponível, consequentemente serão reduzidas a atividade de água e a velocidade das reações químicas no produto, bem como o desenvolvimento de microrganismos (MARTINAZZO et al., 2007;VASCONCELOS, 2015).

Introduction: Lactoferrin (Lf) is a whey protein with a molecular size of about 80 KDa, being found in milk and to a lesser extent in bile and tears. Lf is a cationic molecule with an isoelectric point (pI) around 8.0 to 8.5 having positive charges on its surface which is involved on its biological activity. Lf is a multifunctional protein, very important in the innate immunity system, because it can respond in various ways to physiological changes, present in several studies as preventive and therapeutic treatment, presenting antimicrobial, antifungal, immunomodulatory, antitumor, antiviral activities, as well as neutralization of bioactive substances. This work aimed to purify and characterize lactoferrin from goat milk, monitoring purification by spectroscopy techniques. Materiais and methods: Skimmed milk was obtained by separating the fat from goat milk by centrifugation and subsequent acidified with HCl 0.1 M to pH 4,6 for the casein removal. The acid serum was neutralized with NaOH 0.1 M up to pH 6.8 and then centrifuged (10000 x g, 4° C, 30 min). The supernatant was submitted to saline precipitation profiles of 0-20%, 20-40%, 40-60% and 60-80% saturation of (NH4)2SO4. Fluorimetric analyses salt fractions were performed under excitation length conditions at 290 nm and emission wavelengths between 300-550 nm. Results and discussions:The saline precipitation profiles of 0-20%, 20-40%, 40-60% and 60-80% saturation of (NH4)2SO4 also presented the spectrum of fluorescence characteristic of lactoferrin. However, the profile of the precipitate resuspendido of 40-60% showed the spectrum of fluorescence extinction characteristic of lactoferrin with higher protein concentration. Conclusion: In the present study, it was possible to partially purify lactoferrin caprine using salin tos precipitations with saturation with (NH4)2SO4 being monitored by fluorimetry.

Introduction: Lactoferrin (Lf) is a iron ligating glycoprotein with a molecular mass of approximately 80 kDa, present in mammalian whey, belonging to the transferrin family. Lf can be found in various mucous secretions, such as tears, saliva, gastrointestinal fluids, urine and seminal fluid, as well as in secondary neutrophil granules, being released in places where there is an inflammatory response. Lf is a multifunctional protein possessing functions such as antibacterial, antiviral, antifungal, anti-inflammatory and immunomodulatory activities. This study aimed to purify, characterizing buffalo milk lactoferrin by monitoring the purification by spectroscopic techniques as well as investigating the interaction of protein with antibiotic amoxicillin. Materials and methods: The processing of the buffalo milk began with the separation of fat by centrifugation. The skimmed milk was acidified with HCl 0.1 M up to pH 4.6, obtaining acidified whey and the sour serum was neutralized with NaOH 0.1 M until pH 6.8 and then centrifuged. The supernatant was submitted to saline precipitation profiles of 0-20%, 20-40%, 40-60% and 60-80% saturation of (NH4)2SO4. Fluorimetric analyses of salt fractions were performed under excitation length conditions at 290 nm and emission wavelengths between 300-550 nm. Spectrophotometric studies were carried out with additions of 100 μL of saline fraction 40-60% (0.421 mg/mL), 100 μL of purified lactoferrin (0.421 mg/mL) and 100 μL amoxicillin (2.5x10 -6 mol. L -1 ). Uv-vis absorption spectra were recorded from 190 to 450 nm. Results and discussions:The saline profile of the precipitate was resuspended 40-60% showed the spectrum of fluorescence extinction characteristic of lactoferrin (peak at 332 nm). The 40-60% precipitate was resuspended and submitted to liquid chromatography in a Sephacryl S-100 gel column. Fractions 12 to 16 showed the fluorescence extinction spectrum characteristic of lactoferrin. SDS-PAGE 8%, using commercial lactoferrin (SIGMA) as standard, showed the presence of two protein bands in the standard range. The UV-vis spectrum of maximum absorption showed that the interaction between lactoferrin and amoxicillin play an important role, with the decrease and displacement to the red peak on the UV-vis absorption spectrum when compared with that of lactoferrin partially purified with lactoferrin in the presence of the amoxicillin. Conclusion: Buffalo lactoferrin was partially purify by liquid chromatography in a Sephacryl s-100 resin and SDS-PAGE 8%, using commercial lactoferrin (SIGMA) as standard, showed two protein bands in the standard range. Partially purified buffalo lactoferrin exhibited a UV-vis absorption spectrum with two peaks; the first strong peak centered at absorption maximum in the region 220 to 230 nm is characteristic of the peptide structure and the second peak absorption maximum in the region from 270 to 280 nm due to conjugate double bonds in tyrosine and tryptophan residues. On assays of partial purified Lf incubated with amoxicillin was observed observ...