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Whey protein concentrate hydrolysates, capable of inhibiting the activity of angiotensin-converting enzyme, were prepared in the present study. Several parameters, such as type of enzyme, enzyme:substrate ratio, and use of ultrafiltration were evaluated. The angiotensin-converting enzyme inhibitory activity was observed only after the enzymatic treatment and high rates of inhibition were obtained, ranging from 17.29 to 91.88%. Most hydrolysates obtained with pancreatin showed higher angiotensin-converting enzyme inhibitory activity than those obtained with papain both in the absence and presence of ultrafiltration. The smallest enzyme:substrate ratio for pancreatin resulted in better angiotensin-converting enzyme inhibitory activity values. The use of ultrafiltration proved to be disadvantageous for inhibitory activity of hydrolysates obtained with papain.

In this work, the influence of some reactional parameters in the hydrolysis of whey protein concentrate (WPC) was evaluated, in terms of the nutritional quality of peptide profiles of the hydrolysates as well as the reduction of costs for scaling-up the process. Two enzymes (subtilisin and pancreatin) were used for preparing 18 hydrolysates, using different E:S ratios and reaction times, and the distribution of peptides according to chain length was analyzed by size-exclusion chromatography. The studied parameters affected the peptide profiles of WPC hydrolysates and the best result was similar for subtilisin and pancreatin, both using an E:S ratio of 4:100, after 5 h and 10 h, respectively. In these conditions, these enzymes gave rise to the smallest large peptide contents (12.28% and 12.34%, respectively) and one of the highest amount of di- and tripeptides (13.34% and 13.00%, respectively) as well as of free amino acids (45.56% and 47.26%, respectively). However, in terms of number of samples the action of pancreatin was more advantageous than subtilisin, since among the nine hydrolysates, four showed appropriate peptide profiles (P1, P2, P5, and P6), from the nutritional point of view, while the same happened only with one hydrolysate prepared by using subtilisin (S3). Also, the economical advantage of using smaller E:S ratio and reaction time was observed in several cases for both enzymes.

The aim of this study was to prepare enzymatic hydrolysates from whey protein concentrate with a nutritionally adequate peptide profile and the ability to inhibit angiotensin-converting enzyme (ACE) activity. The effects of the type of enzyme used (pancreatin or papain), the enzyme:substrate ratio (E:S ratio=0.5:100, 1:100, 2:100 and 3:100) and the use of ultrafiltration (UF) were investigated. The fractionation of peptides was performed by size-exclusion-HPLC, and the quantification of the components of the chromatographic fractions was carried out by a rapid Corrected Fraction Area method. The ACE inhibitory activity (ACE-IA) was determined by Reverse Phase-HPLC. All parameters tested affected both the peptide profile and the ACE-IA. The best peptide profile was achieved for the hydrolysates obtained with papain, whereas pancreatin was more advantageous in terms of ACE-IA. The beneficial effect of using a lower E:S ratio on the peptide profile and ACE-IA was observed for both enzymes depending on the conditions used to prepare the hydrolysates. The beneficial effect of not using UF on the peptide profile was observed in some cases for pancreatin and papain. However, the absence of UF yielded greater ACE-IA only when using papain.O objetivo deste estudo foi preparar hidrolisados enzimáticos do concentrado proteico do soro de leite com perfil peptídico nutricionalmente adequado e com capacidade para inibir a atividade da enzima conversora da angiotensina (ECA). Os efeitos do tipo de enzima usado (pancreatina ou papaína), da relação enzima:substrato (E:S=0,5:100, 1:100, 2:100 e 3:100) e do uso da ultrafiltração (UF) foram investigados. O fracionamento dos peptídeos foi feito por CLAE de exclusão molecular e a quantificação dos componentes das frações cromatográficas foi realizada pelo método da Área Corrigida da Fração. A atividade inibitória da ECA (AI-ECA) foi determinada por CLAE de fase reversa. Todos os parâmetros testados afetaram tanto o perfil peptídico quanto a AI-ECA. O melhor perfil peptídico foi atingido para os hidrolisados obtidos com papaína, enquanto a pancreatina foi mais vantajosa em termos da AI-ECA. O efeito benéfico do uso de menor relação E:S sobre o perfil peptídico e a AI-ECA foi observado para ambas as enzimas dependendo das condições usadas para o preparo dos hidrolisados. O efeito benéfico da ausência da UF sobre o perfil peptídico foi observado em alguns casos para pancreatina e papaína. No entanto, a ausência da UF produziu maior AI-ECA somente quando a papaína foi usada.

Visando o aproveitamento de um subproduto industrial e contribuir, assim, para reduzir a poluiçãoambiental, este trabalho teve como objetivo a obtenção de hidrolisados protéicos com elevado teor de ditripeptídeos,a partir do soro de leite. Para tal, empregou-se a pancreatina e diferentes condições hidrolíticasforam testadas. Avaliaram-se o tempo de hidrólise (5, 10 e 15 h), a relação enzima:substrato (E:S) (1:100, 2:100e 4:100) e a concentração da matéria-prima (10 e 15 %). Caracterizou-se o perfil peptídico pelo fracionamentodos hidrolisados por cromatografia líquida de alta eficiência de exclusão molecular e, para a quantificação doscomponentes das frações cromatográficas, empregou-se o método rápido da Área Corrigida da Fração. Para osparâmetros estudados, observaram-se efeitos variados da pancreatina sobre o perfil peptídico dos hidrolisadossendo que, sob o ponto de vista nutricional, nove hidrolisados apresentaram resultados semelhantes, ou seja,altos teores de di-tripeptídeos (12,11%, em média) e de aminoácidos livres (49,06 %, em média), quandocomparados ao hidrolisado protéico de soro comercial.

Vários hidrolisados enzimáticos de soro de leite foram preparados visando a elevação do teor de oligopeptídeos e a redução de custos para produção em larga escala. Para isso, empregou-se a pancreatina e alguns parâmetros hidrolíticos como o tempo de reação (5, 10 e 15h), a relação E:S (1:100, 2:100 e 4:100) e a concentração do substrato (10 e 15%) foram testados. Os hidrolisados foram fracionados por cromatografia liquida de alta eficiência de exclusão molecular (SEHPLC) e, para a quantificação dos componentes das frações cromatográficas, empregou-se o método rápido da Área Corrigida da Fração. Para os parâmetros estudados, observou-se efeito benéfico sobre o perfil peptídico, sendo que o melhor resultado, associado, principalmente, ao maior teor de oligopeptídeos (49%) e ao menor conteúdo de aminoácidos livres (22%), foi obtido quando se empregou a concentração do substrato a 10%, a relação E:S de 4:100 e o tempo de reação de 10h. Several enzymatic hydrolysates of whey were prepared with the objective of increasing the oligopeptide content and reducing the cost of large scale production. Pancreatin was used and some hydrolytic parameters such as reaction time (5, 10 and 15h), enzyme:substrate ratio (E:S) (1:100, 2:100 and 4:100) and substrate concentration (10 and 15%) were tested. The hydrolysates were fractionated by size-exclusion-HPLC and the rapid corrected fraction area method was used for quantifying the chromatographic fractions. The beneficial effect on the peptide profile was observed in several cases, and it was mainly associated with higher oligopeptide (49%) and lower amino acid (22%) contents, which were obtained for a substrate concentration of 10%, E:S ratio of 4:100 and reaction time of 10h.

Two enzyme assisted processes were studied in this work, protein extraction and hydrolysis, aiming phenylalanine (Phe) removal from corn. For protein extraction, a protease of Bacillus liccheniformis was used and the effect of temperature (55 and 60°C) and time (1, 5, 15 and 24 h) was evaluated. For Phe removal, a pancreatin was used for hydrolyzing corn proteins and the activated carbon (AC) was the adsorbent support. In this case, the influence of several parameters was estimated, such as protein extract concentration, E:S ratio, use of freezedrying, protein: AC ratio and way of using AC. The efficiency of Phe removal was evaluated by second derivative spectrophotometry, measuring the Phe content in the corn flour as well as in the hydrolysates after AC treatment. The results showed that the time and the temperature influenced the protein extraction yield and the best results were obtained at 55°C, after 5 h, 15 h and 24 h of reaction, having reached an average extraction yield of 85.3%. The removal of Phe, changed from 68.63 to 97.55%, and its final concentration from 18.80 to 240.75 mg/100 g hydrolysate. The condition that produced the highest Phe removal was the one using a protein extract concentration = 1%, E:S = 1 or 2%, pH 9, temperature = 25°C, protein: C = 1:88.5, using three types of AC and freezedrying (hydrolysates H1 and H2). However, this condition presents some disadvantages such as the use of freezedrying, which highly raises the process cost, and a non-controlled and non-repeatable reaction. Among the samples with no freezedrying stage and more controllable reaction (H9 and H10), H10 is the best one, since it showed smaller Phe content (149.27 mg/100 g) using three types of AC, which is advantageous from the technical point of view. The reduction of the protein: AC ratio, for these two hydrolysates (H9 and H10) was not beneficial for Phe removal, leading to higher Phe content.