Bioactivity of bovine lung hydrolysates prepared using papain, pepsin, and Alcalase

Abstract

Bovine lung tissue was hydrolyzed using three different proteases, papain, pepsin, or Alcalase, to generate hydrolysates. Hydrolysates showed little antioxidant activity in noncellular or cellular assays. The anti‐inflammatory activity of hydrolysates was assessed in RAW264.7 macrophages and Jurkat T cells. Treatment with the Alcalase hydrolysate significantly decreased the production of the pro‐inflammatory cytokines interleukin (IL)‐6 and IL‐1β in a dose dependent manner in RAW264.7 cells. Nitric oxide production also significantly decreased following treatment with this hydrolysate. The papain hydrolysate decreased IL‐6, IL‐1β, and NO production in RAW264.7 cells and IL‐2 production in Jurkat T cells. However, the decrease was likely due to cytotoxicity of this hydrolysate toward these cell lines. The pepsin hydrolysate had no effect on cytokine production in RAW264.7 cells and only slightly decreased IL‐2 production in Jurkat T cells. Practical applications Meat production generates large amounts of protein rich co‐products, which are often discarded as waste or sold as low value animal feeds. The enzymatic hydrolysis of these protein co‐products may produce hydrolysates that are capable of reducing oxidation or inflammation. Novel hydrolysates were generated from the hydrolysis of bovine lung and results from this study indicate that the hydrolysis of bovine lung using the commercially available protease Alcalase may have potential as an anti‐inflammatory agent.

Evaluation of the Antioxidant and Antimicrobial Activities of Porcine Liver Protein Hydrolysates Obtained Using Alcalase, Bromelain, and Papain

“…The enzyme which provided the best results for ORAC was alcalase. This is in agreement with the results found by other authors in bovine lung hydrolysates, where alcalase achieved higher ORAC activity than papain and pepsin [47]. Better results were also found for alcalase than those found by the mixture of pepsin and pancreatin in chicken skin enzymatic protein hydrolysates (35.0% vs. 33.0%, 95.0% vs. 80.0%, and 3800 vs. 3200 µM Trolox equivalent/g for DPPH, metal chelating effect, and ORAC, respectively).…”

“…This increase of the FRAP activity with longer hydrolysis time was also reported with other protein hydrolysates obtained from meat by-products [49,50]. This behavior was reported in the enzymes studied in the present work and in others, such as flavorzyme [47,48]. Verma et al [10] observed that hydrolysis performed with alcalase and papain increased FRAP activity by 40.0% after 6 h of hydrolysis, while increases of about 76.0% were observed by Chang et al [50] in porcine hemoglobin hydrolysates after 10 h of hydrolysis.…”

“…The lower values of FRAP obtained in alcalase and papain could be due to the lower ability of these liver hydrolysate extracts to reduce ferric ion to its ferrous form. In contrast, other authors found that papain presented better results than those obtained for alcalase and bromelain in bovine blood and lung hydrolysates [47,48]. In addition, the values obtained in FRAP assay showed lower values than those found in other liver hydrolysates [10].…”

Structural and functional properties of food protein-derived antioxidant peptides

“…Furthermore, a novel antioxidant peptide (YD1) purified from a strain of Bacillus amyloliquefaciens has also been reported to demonstrate strong antioxidant properties by reducing nitric oxide and ROS generation and increasing the mRNA and protein levels of antioxidant enzymes such as SOD1, CAT, and GPx‐1 in RAW 264.7 murine macrophage cells (Rahman et al, ). The alcalase hydrolyzate of bovine lung had strong in vitro radical scavenging and iron reducing effects but could not prevent H 2 O 2 ‐induced DNA damage (O'Sullivan, Lafarga, Hayes, & O'Brien, ). However, the lung hydrolyzate presented significant anti‐inflammatory activity when tested in RAW264.7 macrophages by reducing nitric oxide production in addition to decreasing the levels of IL‐6 and IL‐1b, which are pro‐inflammatory cytokines.…”

Sonochemical action and reaction of edible insect protein: Influence on enzymolysis reaction‐kinetics, free‐Gibbs, structure, and antioxidant capacity

“…Hydrolysis of proteins by enzymatic means results in the generation of bioactive peptides (Lin, Deng, & Huang, 2014;O'Sullivan, Lafarga, Hayes, & O'Brien, 2017;Sae-Leaw et al, 2017;Saisavoey, Sangtanoo, Reamtong, & Karnchanatat, 2016), and has been judged most adequate compared to alkaline or acid hydrolysis (Clemente, 2001;McCarthy, O'Callaghan, & O'Brien, 2013;Panyam & Kilara, 1996). This is attributed to the fact that the reaction conditions are controllably milder, product quality is high, and the enzymes/proteases are commercially available (Clemente, 2001;McCarthy et al, 2013;Panyam & Kilara, 1996).…”