Angiotensin Converting Enzyme Inhibitors and Antioxidant Peptides Release During Ripening of Mexican Cotija Hard Cheese

نویسندگان

  • Leticia Hernández-Galán
  • Anaberta Cardador-Martínez
  • Daniel Picque
  • Henry Eric Spinnler
  • Sandra Teresita Martín del Campo
  • Luis Castelazo
  • Sandra Teresita Martín
چکیده

Cotija cheese is an artisanal Mexican cheese produced with raw cow ́s milk. Our objective was to measure the antioxidant and angiotensin converting enzyme (ACE) inhibitory activities of the peptides released during its ripening. For that, Cotija cheeses were ripened 6 months in a chamber at 25 oC without humidity control. Weekly samples were taken to determine acid soluble nitrogen (ASN), non-protein nitrogen (NPN) and ethanol soluble nitrogen (EtOH-SN) indexes, by Kjeldahl method. Antioxidant and ACE inhibitory activities were measured by spectrophotometry and HPLC methods, respectively. Peptides in each nitrogen fraction were determined by HPLC. Our results showed that during ripening of Cotija cheeses peptides with antioxidant and ACE inhibitory activities were released and increased through ripening time reaching a maximum of 79.8 % of 2,2diphenyl-1-picrylhydrazyl (DPPH) discoloration and 100 % of ACE inhibition at the end of ripening. Both activities were highly correlated with the types of peptides present in each fraction.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Enterococcus faecium strain used as an adjunct culture in a starter for kashkaval cheese plays important role to proteolytic processes and release of bioactive peptides during ripening

Correspondence: Zhechko Dimitrov LB-Bulgaricum Plc. R&D Center, Sofia, Bulgaria e-mail: [email protected] ABSTRACT In the present study the potential of preliminary selected strain Enterococcus faecium used as an adjunct culture in starter for kashkaval cheese was evaluated. The strain Enterococcus faecium MH3 was selected among 17 isolates on the basis of its high level of prote...

متن کامل

Selected adjunct cultures remarkably increase the content of bioactive peptides in Bulgarian white brined cheese

Some lactic acid bacteria strains in milk media are capable of releasing bioactive peptides. In this study, we evaluated the angiotensin-converting enzyme (ACE)inhibitory activity of 180 lactic acid bacteria and selected several Lactobacillus helveticus, L. delbrueckii subsp. bulgaricus and L. casei strains that demonstrated strong ACE-inhibitory activity. The aim was to carry out a molecular s...

متن کامل

Hydrolysates of sheep cheese whey as a source of bioactive peptides with antioxidant and angiotensin-converting enzyme inhibitory activities

Enzymatic proteolysis may be employed to release bioactive peptides, which have been investigated for potential benefits from both technological and human health perspectives. In this study, sheep cheese whey (SCW) was hydrolyzed with a protease preparation from Bacillus sp. P7, and the hydrolysates were evaluated for antioxidant and angiotensin I-converting enzyme (ACE)-inhibitory activities. ...

متن کامل

High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins Running title: HP promotes the release of bioactive peptides from lentil proteins

*Manuscript Click here to view linked References 2 ABSTRACT 1 Angiotensin I converting enzyme (ACE) inhibitory and antioxidant peptides are receiving attention 2 due to their beneficial effects in the prevention/treatment of hypertension. The objective was to 3 explore the effect of high hydrostatic pressure (HP) on proteolysis by different proteases and the 4 release of bioactive peptides from...

متن کامل

Peptides derived from Rhopilema esculentum hydrolysate exhibit angiotensin converting enzyme (ACE) inhibitory and antioxidant abilities.

Jellyfish (Rhopilema esculentum) was hydrolyzed using alcalase, and two peptides with angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities were purified by ultrafiltration and consecutive chromatographic methods. The amino acid sequences of the two peptides were identified as VKP (342 Da) and VKCFR (651 Da) by electrospray ionization tandem mass spectrometry. The IC50 val...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2016