Anti-osteoporosis effect and purification of peptides with high calcium-binding capacity from walnut protein hydrolysate

2021 ◽  
Author(s):  
Sun Xiaodong ◽  
Ruan Shiyan ◽  
Yongliang Zhuang ◽  
Sun Liping
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Calcium Binding ◽  
Protein Hydrolysate ◽  
Binding Capacity ◽  
Degree Of Hydrolysis ◽  
Gastrointestinal Digestion ◽  
Simulated Gastrointestinal Digestion ◽  
High Calcium ◽  
Relative Molecular Weight

Walnut protein hydrolysate (WPH) was prepared via simulated gastrointestinal digestion. The degree of hydrolysis (DH), amino acid composition, and relative molecular weight distribution of WPH were analyzed. Results showed that...

The Relationship between the Hydrolysis Degree and Calcium-Binding Capacity of Whey Protein by Enzymatic Hydrolysis

2014 ◽  
Vol 541-542 ◽  
pp. 214-219 ◽  
Author(s):  
Li Na Zhao ◽  
Shao Yun Wang ◽  
Shun Li Huang ◽  
Yi Fan Huang
Keyword(s):  
Enzymatic Hydrolysis ◽  
Whey Protein ◽  
Calcium Binding ◽  
Protein Hydrolysate ◽  
Binding Capacity ◽  
Optimum Process ◽  
Hydrolysis Degree ◽  
High Calcium ◽  
Whey Protein Hydrolysate ◽  
The Relationship

To study the relationship between the hydrolysis degree and calcium-binding capacity of whey protein by enzymatic hydrolysis, the response surface method was firstly used to investigate optimized the hydrolysis conditions of whey protein with protamex and flavorzyme. The optimum process parameters for the whey protein hydrolysis were as follows: Whey protein concentration was 5.0% (w/v), the ratio of protease to whey protein was 4.0% (w/w), the mass ratios of protamex to flavorzyme (w/w) was 2:1, and the reaction temperature was 49 °C. The hydrolysate obtained after the hydrolysis of 7 h, with a hydrolysis degree of 25.92%, possessed the highest Ca-binding capacity of 27.92%. Finally, the relationship between the hydrolysis degree and calcium-binding capacity was established and whey protein hydrolysate with high calcium-binding capacity was prepared, which can provide basic theories for the following optimization of chelation of whey protein hydrolysate with calcium.

Changes in the secondary structures and zeta potential of soybean peptide and its calcium complexes in cell membrane medium

2021 ◽  
Author(s):  
He Liu ◽  
Ying Lv ◽  
Jingting Xu ◽  
Chen Chen ◽  
Shuntang Guo
Keyword(s):  
Enzymatic Hydrolysis ◽  
Cell Membrane ◽  
Zeta Potential ◽  
Calcium Binding ◽  
Binding Capacity ◽  
Secondary Structures ◽  
High Calcium ◽  
Calcium Complexes

In this study, soybean peptides (10-30kDa) with high calcium binding capacity were prepared by enzymatic hydrolysis and ultrafiltration. The results of cell experiments showed that the peptide could transport calcium...

Purification and characterisation of a glutamic acid-containing peptide with calcium-binding capacity from whey protein hydrolysate

2015 ◽  
Vol 82 (1) ◽  
pp. 29-35 ◽  
Author(s):  
Shun-Li Huang ◽  
Li-Na Zhao ◽  
Xixi Cai ◽  
Shao-Yun Wang ◽  
Yi-Fan Huang ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Whey Protein ◽  
Calcium Binding ◽  
Protein Hydrolysate ◽  
Binding Capacity ◽  
Reversed Phase ◽  
Exchange Chromatography ◽  
Binding Peptide ◽  
Whey Protein Hydrolysate

The bioavailability of dietary ionised calcium is affected by intestinal basic environment. Calcium-binding peptides can form complexes with calcium to improve its absorption and bioavailability. The aim of this study was focused on isolation and characterisation of a calcium-binding peptide from whey protein hydrolysates. Whey protein was hydrolysed using Flavourzyme and Protamex with substrate to enzyme ratio of 25 : 1 (w/w) at 49 °C for 7 h. The calcium-binding peptide was isolated by DEAE anion-exchange chromatography, Sephadex G-25 gel filtration and reversed phase high-performance liquid chromatography (RP-HPLC). A purified peptide of molecular mass 204 Da with strong calcium binding ability was identified on chromatography/electrospray ionisation (LC/ESI) tandem mass spectrum to be Glu-Gly (EG) after analysis and alignment in database. The calcium binding capacity of EG reached 67·81 μg/mg, and the amount increased by 95% compared with whey protein hydrolysate complex. The UV and infrared spectrometer analysis demonstrated that the principal sites of calcium-binding corresponded to the carboxyl groups and carbonyl groups of glutamic acid. In addition, the amino group and peptide amino are also the related groups in the interaction between EG and calcium ion. Meanwhile, the sequestered calcium percentage experiment has proved that EG-Ca is significantly more stable than CaCl2 in human gastrointestinal tract in vitro. The findings suggest that the purified dipeptide has the potential to be used as ion-binding ingredient in dietary supplements.

Identification of Casein Phosphopeptides in β-casein and Commercial Hydrolysed Casein by Mass Spectrometry

2006 ◽  
Vol 12 (5) ◽  
pp. 379-384 ◽  
Author(s):  
E. Miquel ◽  
J. A. Gómez ◽  
A. Alegría ◽  
R. Barberá ◽  
R. Farré ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Binding Capacity ◽  
Amino Acid Sequences ◽  
Gastrointestinal Digestion ◽  
Simulated Gastrointestinal Digestion ◽  
Casein Phosphopeptides ◽  
Hydrolysed Casein ◽  
Cluster Sequence

Casein phosphopeptides (CPPs) in commercial hydrolysed casein (CE90CPP) and in β-CN (β-CN) after simulated gastrointestinal digestion (gastric stage pepsin, pH =2, 37°C 2h) and intestinal stage (pancreatic-bile extract, pH =5.2, 37°C 2h) were sequenced by on-line reversed-phase high performance liquid chromatography coupled to electrospray ionisation tandem mass spectrometry (RP-HPLC-ESIMS/MS). In β-CN digest five peptides that contained four to five phosphate groups and the cluster sequence SpSpSpEE (residues 17-21) were identified. All CPPs with one exception β-CN(1-24)4P, had the protein fragment β-CN(1-25)4P, which is one of the main CPPs produced in vivo digestion of casein and the results of in vitro studies showed that this fragment enhanced calcium, iron and zinc absorption. In commercial hydrolysed casein CE90CPP 13 peptides were identified, only one of them, αs2-CN (1-13)3P, contained the cluster sequence SpSpSpEE but all the peptides have one or two phosphoserine residues with mineral binding capacity. These CPPs were shorter (527-2061 Da vs 2966-6512 Da) and less phosphorylated (1-3 P vs 4-5 P) than those released after simulated gastrointestinal digestion of β-CN. In both samples, the potential mineral chelating properties of these peptides in relation to their amino acid sequences and the presence of the phosphorylated cluster are discussed.

scholarly journals Effectiveness of Toothpony (Gazza minuta) protein hydrolysate on reducing oil uptake upon deep-frying

Food Research ◽  
2020 ◽  
Vol 4 (3) ◽  
pp. 805-813
Author(s):  
M.K. Zainol ◽  
R.C. Tan ◽  
Z. Mohd Zin ◽  
M. Danish-Daniel ◽  
Amirrudin Ahmad
Keyword(s):  
Protein Hydrolysate ◽  
Binding Capacity ◽  
Human Consumption ◽  
Degree Of Hydrolysis ◽  
Oil Uptake ◽  
Overall Acceptability ◽  
Meat Content ◽  
Total Food ◽  
Fried Foods ◽  
Oil Binding

Toothpony (Gazza minuta) is not typically used for human consumption due to its small size and low meat content, which is widely used as a fish meal. It is stated to be high in protein content and may be suitable for fish protein hydrolysate (FPH) production. Deepfat fried foods contain significant amounts of fat, in some cases up to one-third of the total food weight after frying. Toothpony FPH with low oil-binding ability may reduce the amount of oil consumed by deep-fried products. The objective of this research was to measure the physicochemical properties of Toothpony FPH and its utilisation in reducing the oil intake of deep-fried food. Toothpony FPH was obtained using the enzymatic method successfully. Batter formulations are prepared by adding 0%, 2%, 4%, 6% and 8% of Toothpony FPH into the sample mixtures. The present study indicates the degree of hydrolysis of Toothpony FPH determined by trichloroacetic acid (TCA) method was found to be 98.02%. Toothpony FPH's molecular weight distributions ranged from 7 to 175kDa and FTIR's transmission spectrum indicated the presence of amide I and amide II compounds (1654 and 1535cm-1 ). Oil binding capacity of Toothpony FPH was found to be low, which was 1.9 g oil/ g protein. This study indicated that 4% of Toothpony FPH produced the optimum amount to be incorporated in batter in order to best reduce oil uptake. In sensory evaluation, deep-fat-fried squid incorporated with 8% of Toothpony FPH showed the highest acceptance in all attributes, which were colour, crispness, oiliness, taste and overall acceptability. This approach offers the potentials use of Toothpony fish FPH for the production batter formulation which is efficient in the reduction of oil uptake.

scholarly journals Effect of Enzymatic Hydrolysis on the Zinc Binding Capacity and in vitro Gastrointestinal Stability of Peptides Derived From Pumpkin (Cucurbita pepo L.) Seeds

2021 ◽  
Vol 8 ◽  
Author(s):  
Dan Lu ◽  
Mengyao Peng ◽  
Min Yu ◽  
Bo Jiang ◽  
Hong Wu ◽  
...  
Keyword(s):  
Particle Size ◽  
Enzymatic Hydrolysis ◽  
Protein Hydrolysate ◽  
Binding Capacity ◽  
Average Molecular Weight ◽  
Zinc Binding ◽  
Degree Of Hydrolysis ◽  
Pumpkin Seed ◽  
Binding Behavior

Zinc is a crucial micronutrient for maintaining body immune system and metabolism function. However, insufficient intake from diet may lead to zinc deficiency and impair normal body function. In addition, conventional zinc salts supplementation has the disadvantage of low bioavailability since the zinc ions may be easily chelated by dietary fiber or phytate commonly found in diets rich in plants, and form precipitates that cannot be absorbed. Therefore, the objective of the present study is to prepare pumpkin seed derived peptides and to evaluate the effect of structure and surface properties on the zinc binding behavior of the pumpkin seed protein hydrolysate (PSPH), as well as their gastrointestinal stability. Briefly, different PSPHs were prepared using enzymatic hydrolysis method with bromelain, papain, flavourzyme, alcalase, and pepsin. The particle size, zeta potential, surface hydrophobicity, degree of hydrolysis, ATR-FTIR spectra, and zinc binding capacity were determined. The representative samples were chosen to characterize the binding energy and surface morphology of PSPH-Zn. At last, the in vitro gastrointestinal stability of PSPH and PSPH-Zn were evaluated. Our results showed that peptides hydrolyzed by papain had the largest average molecular weight, smallest particle size, highest hydrophobicity, and the greatest zinc binding capacity. Zinc showed better gastrointestinal stability in PSPHs chelates than in its salt. Meanwhile, PSPH-Zn with higher zinc binding capacity showed better stability. The result of this study indicated pumpkin seed hydrolyzed by papain may be used as a potential source for zinc fortification. The findings in this study may provide important implications for developing plant-based zinc chelating peptides.

Biochemical and histochemical characteristics of proteins homologous to calf lens membrane proteins with high calcium-binding capacity

1985 ◽  
Vol 159 (2) ◽  
pp. 519-530 ◽  
Author(s):  
A.J.M. Van den Eijnden-van Raaij ◽  
A.L.M. De Leeuw ◽  
H.J. Winkens ◽  
J.F.J. Kruisselbrink-Borgonjen ◽  
R.M. Broekhuyse
Keyword(s):  
Membrane Proteins ◽  
Calcium Binding ◽  
Binding Capacity ◽  
High Calcium
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