Role of indigenous enzymes in proteolysis of casein in caprine milk

Santillo, Antonella; Kelly, Alan L.; Palermo, Carmen; Sevi, A.; Albenzio, Marzia

doi:10.1016/j.idairyj.2009.06.011

Cited by 29 publications

(23 citation statements)

References 31 publications

(40 reference statements)

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“…Caprine milk contains the entire plasmin system: plasmin, plasminogen, plasmin inhibitors, plasminogen activators, and inhibitors of plasminogen activators (Trujillo et al 1997). Santillo et al (2009) reported that plasmin mainly contributed to hydrolysis of β-casein in caprine milk, analogously for bovine milk.…”

Section: Comparison Of the 2-de Patterns And Identification Of Proteimentioning

confidence: 99%

Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk

Hinz

O’Connor

Huppertz

et al. 2012

Journal of Dairy Research

130

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Proteomic analysis of bovine, caprine, buffalo, equine and camel milk highlighted significant interspecies differences. Camel milk was found to be devoid of β-lactoglobulin, whereas β-lactoglobulin was the major whey protein in bovine, buffalo, caprine, and equine milk. Five different isoforms of κ-casein were found in camel milk, analogous to the micro-heterogeneity observed for bovine κ-casein. Several spots observed in 2D-electrophoretograms of milk of all species could tentatively be identified as polypeptides arising from the enzymatic hydrolysis of caseins. The understanding gained from the proteomic comparison of these milks may be of relevance both in terms of identifying sources of hypoallergenic alternatives to bovine milk and detection of adulteration of milk samples and products.

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Section: Comparison Of the 2-de Patterns And Identification Of Proteimentioning

confidence: 99%

Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk

Hinz

O’Connor

Huppertz

et al. 2012

Journal of Dairy Research

130

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“…We also obtained a 672 Da peptide, previously described by Gómez-Ruiz et al (2008), which has [GLDIQK] sequence and is known by its antihypertensive properties. Another one was a 760 Da peptide, described by Santillo et al (2009) who characterized it as a f(205-223) αs 2 -casein, whose sequence is [K.AMKPWTQPKTNAIPYVRY]. These authors determined its antihypertensive property.…”

Section: Peptide Profile and Amino Acids Sequencing From Casein Hydromentioning

confidence: 99%

“…Silva and Araújo (2000) pointed out that the exploitation of Moxotó caprine milk, in regards to human nutrition and milk derivatives production, is underexplored, although the utilization of goat milk peptides has an attractive potential in food industry. Caprine milk consumption is important owing to its beneficial nutritional characteristics such as large concentration of proteins with high DH nutritional value and potential use by people allergic to bovine milk (SANTILLO et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

Biotechnological richness of the northeastern semi-arid region: antioxidant activity of casein hydrolysates from Moxotó goat milk (Capra hircus Linnaeus, 1758) obtained by papain action

et al. 2013

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“…O estudo das propriedades funcionais e nutricionais dos produtos lácteos é estratégia adequada para melhor aproveitamento do leite caprino (Santillo et al, 2009). As características peculiares do leite de cabra, do ponto de vista nutricional e social, motivam pesquisas para avaliação de aspectos produtivos e qualitativos de sua produção (Fernandes et al, 2008).…”

Section: Introductionunclassified

“…Há crescente interesse pela utilização desse produto como alimento funcional, em consonância com a atual tendência de alimentação saudável (Olalla et al, 2009). Entre as características nutricionais benéficas do leite de cabra, destacam-se a elevada concentração de proteínas de alto valor nutritivo e a possível utilização desse leite por pessoas alérgicas ao leite de vaca (Olalla et al, 2009;Santillo et al, 2009).…”

Section: Introductionunclassified

Avaliação de variáveis que influenciam a hidrólise enzimática da caseína do leite de cabra Moxotó

Lira

Bezerra

Silva

et al. 2010

Pesq. agropec. bras.

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Resumo − O objetivo deste trabalho foi avaliar os efeitos da temperatura, pH, relação enzima:substrato (E:S) e tempo de reação sobre a hidrólise enzimática da caseína do leite de cabra Moxotó, com uso de diferentes enzimas proteolíticas. A hidrólise enzimática da caseína caprina foi realizada com uso de tripsina, pepsina e papaína. Para cada enzima, foram utilizados dois níveis de cada variável, na avaliação de seus efeitos sobre a hidrólise da caseína, em um fatorial completo 2 4 . Os produtos da hidrólise foram visualizados em eletroforese SDS-PAGE. O melhor valor do grau de hidrólise com a enzima papaína foi obtido em pH 6,5, E:S de 1:150 e 5 horas de hidrólise a 50ºC (28,17%); com a tripsina, em pH 8,5, E:S de 1:150 e 5 horas a 40ºC (29,55%); e com a pepsina, em pH 3,0, E:S de 1:100 e 5 horas a 40ºC (38,27%). A hidrólise da caseína caprina é influenciada positivamente pelo pH e tempo de hidrólise, com o uso da pepsina. Foram observadas interações significativas antagônicas entre pH e relação E:S, com o uso da tripsina; e entre pH, temperatura e tempo de hidrólise, com o uso da papaína. A pepsina apresenta elevada eficiência na hidrólise de α s1 , β e κ-caseína, evidenciada por hidrolisados com massa molar abaixo de 14,4 kDa.Termos para indexação: Capra hircus, leite de cabra, papaína, pepsina, proteólise, tripsina. Evaluation of the variables that influence the enzymatic hydrolysis of Moxotó goat's milk caseinAbstract -The aim of this work was to evaluate the effects of temperature, pH, enzyme:substrate ratio (E:S), and reaction time on the enzymatic hydrolysis of Moxotó breed goat's milk casein, using different proteolytic enzymes. Enzymatic hydrolysis of the capric casein was performed using trypsin, pepsin and papain. For each enzyme, two levels of the variables were used to assess their effects on the hydrolysis of casein, using a full factorial design (2 4 ). The hydrolysis products were visualized on SDS-PAGE. The best hydrolysis degree using papain were at pH 6.5, E:S of 1:150 and 5 hours of hydrolysis at 50°C (28.17%); for trypsin, at pH 8.5, E:S of 1:150 and 5 hours at 40°C (29.55%); and for pepsin, at pH 3.0, E:S of 1:100 and 5 hours at 40°C (38.27%). Capric casein hydrolysis is affected positively by pH and reaction time, using pepsin. Significant antagonistic interactions were observed between pH and E:S, with trypsine; and between pH, temperature and reaction time, with papain. Pepsin has high α s1 , β e κ-casein hydrolysis efficiency, evidenced by the molar masses below 14.4 kDa of its products.

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Role of indigenous enzymes in proteolysis of casein in caprine milk

Cited by 29 publications

References 31 publications

Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk

Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk

Biotechnological richness of the northeastern semi-arid region: antioxidant activity of casein hydrolysates from Moxotó goat milk (Capra hircus Linnaeus, 1758) obtained by papain action

Avaliação de variáveis que influenciam a hidrólise enzimática da caseína do leite de cabra Moxotó

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