Application of Proteases for the Production of Bioactive Peptides

Chew, Lye Yee; Toh, Gaik Theng; Ismail, Amin

doi:10.1016/b978-0-12-813280-7.00015-3

Cited by 33 publications

(29 citation statements)

References 25 publications

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“…Yeast are also rich in endogenous nucleases and proteases that can degrade nucleic acids, DNA, and RNA into nucleotides through autolysis (71,72). By controlling pH, temperature, and duration as well as use of additives such as salt and exogenous enzymes, the yeast cell autolysis can be an optimized and standardized for consistent product quality (73). These modifications are increasingly being used to produce yeast nucleotide products for various industrial application.…”

Section: Nucleotidesmentioning

confidence: 99%

“…These modifications are increasingly being used to produce yeast nucleotide products for various industrial application. For example, under normal autolysis conditions, the RNA is mainly degraded to three primary nucleotides, however, under controlled enzymatic hydrolysis, 5 prime nucleotides of guanine, adenine, cytosine and uracil are produced (73,74).…”

Section: Nucleotidesmentioning

confidence: 99%

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Utility of Feed Enzymes and Yeast Derivatives in Ameliorating Deleterious Effects of Coccidiosis on Intestinal Health and Function in Broiler Chickens

et al. 2019

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Section: Nucleotidesmentioning

confidence: 99%

Section: Nucleotidesmentioning

confidence: 99%

Utility of Feed Enzymes and Yeast Derivatives in Ameliorating Deleterious Effects of Coccidiosis on Intestinal Health and Function in Broiler Chickens

et al. 2019

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“…However, microbial proteases are preferred due to technical and economic advantages (Singh, Mittal, Kumar, & Mehta 2016). In addition, enzyme‐assisted processing does not give rise to safety and health issues, and it is considered as a green process without detrimental impacts to the environment (Chew et al., 2019).…”

Section: Introductionmentioning

confidence: 99%

Multifunctional in vitro bioactive properties: Antioxidant, antidiabetic, and antihypertensive of protein hydrolyzates from tarwi (Lupinus mutabilis Sweet) obtained by enzymatic biotransformation

et al. 2020

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Background and objectives Tarwi is a legume that grows in the Andean region of Peru. This grain is characterized by having a high protein content (~42%). In order to generate added‐value products from this resource, the possibility of obtaining tarwi protein hydrolyzates (TPH) with in vitro bioactive properties was evaluated using Alcalase, Neutrase, and Flavourzyme enzymes, acting alone or in combination for up to 240 min. The in vitro evaluated properties were as follows: antioxidant (ABTS assay), antidiabetic (α‐amylase, α‐glucosidase and dipeptidyl peptidase IV (DPP‐IV) inhibition), and antihypertensive (angiotensin‐converting enzyme‐I (ACE) inhibition). Findings The TPH obtained from the different enzyme treatments exhibited important antioxidant, antidiabetic (specially for DPP‐IV inhibition), and antihypertensive properties. One‐stage treatment using Alcalase for 240 min and two sequential stage treatments with Alcalase–Neutrase for 180 min presented the highest ABTS antioxidant activity and lowest IC50 values for DPP‐IV and ACE corresponding to 2.0–1.95 µmol TE/mg, 2.14–2.61 and 0.16–0.11 mg/ml, respectively. Conclusions The results of this research demonstrate that TPH exhibit in vitro multifunctional bioactive properties. Significance and novelty TPH could potentially be used in the prevention or management of chronic diseases related to the development of oxidative processes, diabetes, and hypertension.

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“…The largest known family of proteases is serine proteases [ 5 ]. In general, proteases play key roles in different physiological processes in all living organisms, including replication, transcription, cell proliferation, cell migration, tissue morphogenesis, release of hormones and pharmacologically active peptides, apoptosis, and wound healing [ 1 , 6 , 7 ].…”

Section: Introductionmentioning

confidence: 99%

Purification and Biochemical Characterization of a New Protease Inhibitor from Conyza dioscoridis with Antimicrobial, Antifungal and Cytotoxic Effects

et al. 2020

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The main objective of the current study was the extraction, purification, and biochemical characterization of a protein protease inhibitor from Conyzadioscoridis. Antimicrobial potential and cytotoxic effects were also examined. The protease inhibitor was extracted in 0.1 M phosphate buffer (pH 6–7). Then, the protease inhibitor, named PDInhibitor, was purified using ammonium sulfate precipitation followed by filtration through a Sephadex G-50 column and had an apparent molecular weight of 25 kDa. The N-terminal sequence of PDInhibitor showed a high level of identity with those of the Kunitz family. PDInhibitor was found to be active at pH values ranging from 5.0 to 11.0, with maximal activity at pH 9.0. It was also fully active at 50 °C and maintained 90% of its stability at over 55 °C. The thermostability of the PDInhibitor was clearly enhanced by CaCl2 and sorbitol, whereas the presence of Ca2+ and Zn2+ ions, Sodium taurodeoxycholate (NaTDC), Sodium dodecyl sulfate (SDS), Dithiothreitol (DTT), and β-ME dramatically improved the inhibitory activity. A remarkable affinity of the protease inhibitor with available important therapeutic proteases (elastase and trypsin) was observed. PDInhibitor also acted as a potent inhibitor of commercial proteases from Aspergillus oryzae and of Proteinase K. The inhibitor displayed potent antimicrobial activity against gram+ and gram- bacteria and against fungal strains. Interestingly, PDInhibitor affected several human cancer cell lines, namely HCT-116, MDA-MB-231, and Lovo. Thus, it can be considered a potentially powerful therapeutic agent.

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Application of Proteases for the Production of Bioactive Peptides

Cited by 33 publications

References 25 publications

Utility of Feed Enzymes and Yeast Derivatives in Ameliorating Deleterious Effects of Coccidiosis on Intestinal Health and Function in Broiler Chickens

Utility of Feed Enzymes and Yeast Derivatives in Ameliorating Deleterious Effects of Coccidiosis on Intestinal Health and Function in Broiler Chickens

Multifunctional in vitro bioactive properties: Antioxidant, antidiabetic, and antihypertensive of protein hydrolyzates from tarwi (Lupinus mutabilis Sweet) obtained by enzymatic biotransformation

Purification and Biochemical Characterization of a New Protease Inhibitor from Conyza dioscoridis with Antimicrobial, Antifungal and Cytotoxic Effects

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