Mahta Mirzaeia, Saeed Mirdamadib, Mohamad Reza Ehsani, Mahmoud Aminlarid
Functional Foods in Health and Disease 2016; 6(7): 425-439

Background: There has been some evidence that proteins are potentially excellent source of antioxidants, antihypertensive and antimicrobial peptides and enzymatic hydrolysis is an effective method to release these peptides from protein molecules. The functional properties of protein hydrolysates depends on the protein substrate, the specificity of the enzymes, the conditions used during proteolysis, degree of hydrolysis, and the nature of peptides released including molecular weight, amino acid composition, and hydrophobicity.

Context and purpose of this study: The biomass of Kluyveromyces marxianus was considered as a source of ACE inhibitory, antioxidant and antimicrobial peptides.

Results: Autolysis and enzymatic hydrolysis were completed respectively, after 96 h and 5 h. Overall, trypsin (18.52% DH) and chymotrypsin (21.59% DH) treatments were successful in releasing antioxidant and ACE inhibitory peptides. Autolysate sample (39.51% DH) demonstrated a poor antioxidant and ACE inhibitory activity compared to trypsin and chymotrypsin hydrolysates. The chymotrypsin 3-5 kDa (301.6±22.81 μM TEAC/mg protein) and trypsin< 3 kDa (280.16±39.16) permeate peptide fractions showed the highest DPPH radical scavenging activity. The trypsin <3 kDa permeate peptide fraction showed the highest ABTS radical scavenging (1691.1±48.68 μMTE/mg protein) and ACE inhibitory (IC50=0.03±0.001 mg/ml) activities. The fraction (MW=5-10 kD) obtained after autolysis treatment showed antibacterial activity against St. aureus and Lis. monocytogenes in well diffusion screening. The minimum inhibitory concentration (MIC) value was 13.3 mg/ml against St. aureus and Lis. monocytogenes calculated by turbidimetric assay and it showed bactericidal activity against St. aureus at 21.3 mg/ml protein concentration.

Conclusions: Taken together, the results of this study reveal that K. marxianus proteins contain specific peptides in their sequences which can be released by enzymatic hydrolysis and autolysis.


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