Identification, characterization and in vitro activity of hypoglycemic peptides in whey hydrolysates from rubing cheese by-product

Li, Yiyan; Fan, Yaozhu; Liu, Jinglei; Meng, Zishu; Huang, Aixiang; Xu, Feiran; Wang, Xuefeng

doi:10.1016/j.foodres.2022.112382

Cited by 12 publications

(4 citation statements)

References 44 publications

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“…Rushan cheese whey hydrolysates (RCWH) were prepared based on the method of Li et al (2023) with slight modifications. Briefly, 1 g of whey powder was added to 30 mL of ultrapure water and stirred (IKA Werke GmbH & Co. KG, Staufen, Germany) at 25 °C for 4 h. Then, 0.04 g of papain was added to the mixture and incubated at 50 °C and pH 8.0 at 4 h. After hydrolysis, the enzyme was inactivated by heating at 95 °C for 10 min.…”

Section: Methodsmentioning

confidence: 99%

Identification, structural characterization, and molecular dynamic simulation of ACE inhibitory peptides in whey hydrolysates from Chinese Rushan cheese by-product

Wei,

Wang,

et al. 2024

Food Chemistry: X

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Section: Methodsmentioning

confidence: 99%

Identification, structural characterization, and molecular dynamic simulation of ACE inhibitory peptides in whey hydrolysates from Chinese Rushan cheese by-product

Wei,

Wang,

et al. 2024

Food Chemistry: X

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“…It was reported that smaller peptides may be more active than bigger peptides [28]. In addition, Félix-Medina et al [29] and Li et al [30] found that a better hypoglycemic activity of peptide fractions was observed as their molecular weights decreased. Moreover, Wang et al [31] discovered that most peptides possessing antihyperglycemic activity have molecular weights below 1 kDa.…”

Section: Introductionmentioning

confidence: 97%

“…Meanwhile, their α-GIA could remain 100% at temperatures of 20, 40, and 60 • C, then quickly decreased to 18.73% at 100 • C [31]. On the other hand, the α-GIA of YPVEPF (a hypoglycemic peptide identified from whey hydrolysate) increased up to 4 times at pH = 2, and it reduced by approximately 9 times at pH = 10 [30]. Besides, this peptide was found to be stable at the temperature range of 20-80 • C, with its highest α-GIA retention rate of 94% at 60 • C [30].…”

Section: Introductionmentioning

confidence: 99%

Earthworm (Perionyx excavatus) Protein Hydrolysate: Hypoglycemic Activity and Its Stability for the Hydrolysate and Its Peptide Fractions

Bui,

Pham,

2023

Processes

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This study aims at exploring earthworm protein hydrolysate and its peptide fractions as a potential hypoglycemic agent by inhibiting α-amylase and α-glucosidase. Firstly, the best hydrolysis conditions to gain the hydrolysates with the highest α-amylase inhibitory activity (α-AIA) and α-glucosidase inhibitory activity (α-GIA) were figured out using a one-factor test. Next, the stability of the hypoglycemic activity of the hydrolysates and their 5 peptide fractions recovered using ultrafiltration membranes were assessed by employing the tests of in vitro digestion, thermal, and pH treatment. The results showed that at the best hydrolysis conditions, the hydrolysates exhibited α-AIA of 91.30 ± 2.51% and α-GIA of 44.69 ± 0.47%. Specifically, the <1 kDa peptide fraction from the hydrolysate expressed a greater α-AIA than that of acarbose, with nearly the same α-GIA as that of voglibose. The α-AIA and α-GIA of the hydrolysates and their fractions were enhanced after the in vitro digestion treatment, whereas they remained over 40% after the pH treatment in the range of 1 to 11 or heat treatment at 100 °C for 180 min. These data provide the preliminary evidence to develop the earthworm protein hydrolysate and its peptide fractions in functional food or nutraceutical products with hypoglycemic activity.

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“…As there is a high content of collagen in fish scales, utilizing it can not only reduce the damage to the environment but also increase the potential income of the aquaculture industry [ 4 ]. After enzymatic hydrolysis, collagen can form collagen peptides with different molecular sizes and certain biological activities, such as antifreeze, anti-inflammatory and hypoglycemic activity, as well as other functionally active peptides [ 5 , 6 , 7 ]. At present, the extraction of collagen peptides from natural substances has been widely studied and aquatic animals have the advantages of low resistance and allergenicity.…”

Section: Introductionmentioning

confidence: 99%

Silver Carp (Hypophthalmichthys molitrix) Scales Collagen Peptides (SCPs): Preparation, Whitening Activity Screening and Characterization

Xiaoyan

Xiong

et al. 2023

Foods

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This study involves the preparation of scale collagen peptides (SCPs) with whitening activity from silver carp (Hypophthalmichthys molitrix) and their characterization and peptide sequence identification. In this article, scanning electron microscopy (SEM) was used to observe structure changes of sliver carp scales; enzymatic hydrolysis was optimized through protease screening and response surface optimization. The ultrafiltration was used to separate SCPs and the whitening activity was comprehensively evaluated using radical scavenging rate and tyrosinase-inhibiting activity, among others. An optimal component was characterized and identified using various modern spectral analysis techniques. The results showed that the surface of silver carp scales after decalcification was smooth and clear. The pepsin had the highest peptide yield and tyrosinase-inhibiting activity (90.01% and 82.25%, respectively). The optimal enzymatic hydrolysis conditions were an enzyme dosage of 16.1%, a solid–liquid ratio of 1:15.6 and a time of 4.9 h. The proportions of hydrophobic and basic amino acids in the peptide composition were 32.15% and 13.12%, respectively. Compared with SCPs2, SCPs1 (6096.68–9513.70 Da) showed better ·OH scavenging ability, tyrosinase-inhibiting activity and moisture absorption. SCPs1 was a macromolecular fragment of type I collagen with a triple helix structure, containing three peptide sequences with the potential for tyrosinase activity inhibition (AGPPGADGQTGQRGE, SGPAGIAGPAGPRGPAGPNGPPGKD and KRGSTGEQGSTGPLGMRGPRGAA). These results show that SCPs1 is a collagen peptide product with whitening potential.

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Identification, characterization and in vitro activity of hypoglycemic peptides in whey hydrolysates from rubing cheese by-product

Cited by 12 publications

References 44 publications

Identification, structural characterization, and molecular dynamic simulation of ACE inhibitory peptides in whey hydrolysates from Chinese Rushan cheese by-product

Identification, structural characterization, and molecular dynamic simulation of ACE inhibitory peptides in whey hydrolysates from Chinese Rushan cheese by-product

Earthworm (Perionyx excavatus) Protein Hydrolysate: Hypoglycemic Activity and Its Stability for the Hydrolysate and Its Peptide Fractions

Silver Carp (Hypophthalmichthys molitrix) Scales Collagen Peptides (SCPs): Preparation, Whitening Activity Screening and Characterization

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