Evaluation of Antidiabetic Activities of Casein Hydrolysates by a Bacillus Metalloendopeptidase
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Evaluation of Antidiabetic Activities of Casein Hydrolysates by a Bacillus Metalloendopeptidase Sarah Megrous1 · Sam Al‑Dalali1 · Xiao Zhao1 · Chao Chen2 · Yongqiang Cao2 · Imane Bourouis1 · Aicha Mekkaoui1 · Zhijie Yang1 · Zhennai Yang1,2 Accepted: 4 February 2020 © Springer Nature B.V. 2020
Abstract Enzymatic hydrolysis is commonly used to produce bioactive peptides from protein such as casein that is rich in bioactive peptide sequences. In this study, a Bacillus metalloendopeptidase (PROTIN SD-NY10) was used to hydrolyze casein to produce bioactive peptides with antidiabetic and antioxidant activities. Several factors affecting the hydrolysis were assessed such as hydrolysis time, metalloendopeptidase concentration, casein concentration, pH, and temperature. The results showed that casein could be effectively hydrolyzed by the metalloendopeptidase, and the casein hydrolysates were shown with high inhibitory activities on α-glucosidase and α-amylase, as well as high antioxidant activity. The high inhibitory activities on α-glucosidase (68.5–80.55%) and α-amylase (74.10–77.15%) were obtained under the selected hydrolysis conditions (pH 7.5, 40 °C, 1% metalloendopeptidase, 10% casein, and 3 h). Meanwhile, the high DPPH radical scavenging activity (55.02–69.40%) could also be obtained under the same hydrolysis conditions. Therefore, the casein hydrolysate obtained by hydrolysis with a metalloendopeptidase of this study could be explored as a bioactive agent for potential application in functional products. Keywords Metalloendopeptidase · Casein hydrolysate · Antidiabetic · Antioxidant
Introduction As the main component of milk protein, casein represents about 80% of milk protein, and it has many applications in nutrition, health, and industrial food application (De Oliveira et al. 2018). Casein contains several fractions including αs1-, αs2-, β- and κ-casein with distinct peptide sequences, which can be released as a result of proteolysis, exhibiting distinctive biological activities (Benkerroum 2010; Hartmann and Meisel 2007; Madureira et al. 2010). These peptides, containing 3 to 20 amino acids, had hormone-like activity, antimicrobial activity, cytomodulatory, immunomodulatory, * Zhennai Yang [email protected] 1
Beijing Advanced Innovation Center for Food Nutrition and Human Health, Beijing Engineering and Technology Research Center of Food Additives, Beijing Technology and Business University, Beijing 100048, People’s Republic of China
Dongjun Dairy (Yucheng) Co., Ltd., Yucheng 251200, People’s Republic of China
2
antioxidant, blood-pressure lowering (“Angiotensin-converting enzyme ACE-inhibitory”), and opioid like activities (Dziuba and Darewicz 2007; McCarthy et al. 2014; Pihlanto 2001; Teschemacher et al. 1997). Hydrolysis of protein can be conducted by different methods, including chemical treatment, microbial fermentation or enzymatic hydrolysis (Sánchez and Vázquez 2017). Enzymatic hydrolysis is the most commonly used method to generate bioactive peptides (BAPs) from the original prot
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