Seabuckthorn (Hippophae rhamnoides L.), a novel seed protein concentrate: isolation and modification by high power ultrasound and characterization for its functional and structural properties

Khan, Zakir Showkat; Sodhi, Navdeep Singh; Dhillon, Bhavnita; Dar, B.N.; Bakshi, Rayees Ahmad; Shah, Shemilah Fayaz

doi:10.1007/s11694-021-01020-7

Cited by 12 publications

(25 citation statements)

References 34 publications

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“…Seabuckthorn seed protein solution (10% w/v) was placed in a jacketed beaker with ice on the outside to maintain the temperature and ultrasonicated using an Ultrasonic processor (CP‐500, Illinois, USA) with a pulse of 1 s, frequency of 24 kHz at an amplitude of 50% for different periods of 15, 45 and 75 min in accordance with our previous studies (Khan et al ., 2021). The samples were named as SSPC 15, SSPC 45 and SSPC 75 respectively.…”

Section: Methodsmentioning

confidence: 99%

“…Preparation of SSPC hydrolysates using pepsin, trypsin and protamex SSPC hydrolysates were prepared according to our recent study (Khan et al, 2021). The protein dispersions were incubated at optimum catalytic temperature and pH conditions for individual enzymes (pepsin, trypsin and protamex).…”

Section: Ultrasonication Of Sspc Proteinmentioning

confidence: 99%

“…Various recent studies have reported that enzymatic modification improves plant protein functionality to a great extent (Galante et al ., 2020; Wang et al ., 2022). Different enzymes used to modify required protein functionality are pepsin, trypsin, papain, alcalase and protamex (Khan et al ., 2021). Hydrolysis of proteins using enzymes can improve their emulsifying properties due to the exposure of more hydrophobic groups, flexibility in mobility and molecular weight (Jin et al ., 2020; Yan et al ., 2021).…”

Section: Introductionmentioning

confidence: 99%

“…Protein content ranges from 46 to 129 g/kg for various Seabuckthorn species in India (Ranjith et al ., 2006; Marsinach & Cuenca, Marsiñach & Cuenca, 2019). A significant portion of protein in Seabuckthorn berry is present in its seeds (Uransanaa et al ., 2003; Khan et al ., 2021) and can be utilised for various food applications (Khan et al ., 2021). In our recent studies (Khan et al ., 2021) we found that functional properties of Seabuckthorn seed protein concentrate like solubility, surface hydrophobicity and emulsifying activity index is improved by ultrasonication and enzymatic hydrolysis.…”

Section: Introductionmentioning

confidence: 99%

“…A significant portion of protein in Seabuckthorn berry is present in its seeds (Uransanaa et al ., 2003; Khan et al ., 2021) and can be utilised for various food applications (Khan et al ., 2021). In our recent studies (Khan et al ., 2021) we found that functional properties of Seabuckthorn seed protein concentrate like solubility, surface hydrophobicity and emulsifying activity index is improved by ultrasonication and enzymatic hydrolysis. Therefore, the objective of this study was to investigate the effect of ultrasonication and enzymatic hydrolysis using pepsin, trypsin and protamex on emulsifying stability of Seabuckthorn seed protein concentrate.…”

Section: Introductionmentioning

confidence: 99%

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Seabuckthorn seed protein concentrate: a novel seed protein; emulsifying properties as affected by ultrasonication and enzymatic hydrolysis

Khan

Sodhi²,

Fayaz

et al. 2022

Int J of Food Sci Tech

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The study investigated the influence of ultrasonication and enzymatic hydrolysis on emulsifying properties of Seabuckthorn seed protein concentrate (SSPC). Sonication was done at 24 kHz (50% amplitude) for different time combinations (15, 45 and 75 min), and enzymatic hydrolysis of SSPC was done using pepsin, trypsin and protamex, resulting in different SSPC emulsions. All the emulsions were characterised to ascertain the particle size distribution, pH stability, temperature stability and rheology. Hydrolysed SSPC was also characterised for the respective degree of hydrolysis by pepsin, trypsin and protamex. The pepsin revealed the highest degree of hydrolysis among the proteases, followed by trypsin and protamex. The ultrasonicated SSPC and SSPC hydrolysate emulsions showed unimodal particle size distribution except for pepsin hydrolysate emulsions which showed bimodal size distribution of particles. The variation in pH from 2 to 5 increased the particle size, while at higher pH (7-10), the particle size decreased for all the emulsions. The increase in temperature from 25°C to 85 °C increased the droplet size of all the emulsions except for protamex at 75 min, which showed a relatively smaller droplet size than other proteases. All the emulsions displayed shear thinning behaviour, however, the pepsin-treated emulsions showed the highest consistency index and K-value. The resulting ultrasonicated and different protease-treated SSPC emulsions can be suitable green and nontoxic alternatives to synthetic emulsifiers used in the food industry.

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Section: Methodsmentioning

confidence: 99%

Section: Ultrasonication Of Sspc Proteinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Seabuckthorn seed protein concentrate: a novel seed protein; emulsifying properties as affected by ultrasonication and enzymatic hydrolysis

Khan

Sodhi²,

Fayaz

et al. 2022

Int J of Food Sci Tech

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Valorization of sea buckthorn seed protein to hydrolysates: Impact on morphological, structural, functional, and antioxidant properties

et al. 2023

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Background: Increasing concerns about nutritional deficiency, food security, and sustainability have emphasized work on exploring alternative and sustainable sources of protein. In this study, an initiative to extract and utilize protein concentrates, and hydrolysates from sea buckthorn seed, otherwise a waste material, is undertaken. The effect of hydrolysis using various enzymes namely pepsin (pH 2.0 and 37 C), trypsin (pH 7.0 and 37 C), and protamex (pH 7.0 and 50 C), for different time durations, namely, 30, 60, 90, and 120 min, on the structural and functional properties of sea buckthorn seed protein concentrate (SSPC), was elucidated. Results:The emulsifying activity index and solubility of pepsin-hydrolysed SSPC increased significantly and were higher than those of trypsin and protamex hydrolysed SSPC samples. A Fourier transformation infrared study revealed that the enzyme hydrolysis treatment reduced the peak intensity in amide I, II, and III bands. A significant change was found in the β-sheet, β-turn and random coiling of the secondary structure of SSPC protein by enzymatic hydrolysis. The particle size ranged from 295.8 to 440, 388 to 713.6, 399 to 890 nm for pepsin, trypsin, and protamex, respectively. The microstructure of pepsin-treated samples showed a more porous and loose structure than native, trypsin and protamex. Antioxidant activity increased significantly for all the samples with enzyme treatments carried out for different periods. Conclusion:The results indicate that the protein-rich hydrolysates could create new opportunities for the development of effective techno-functional additives for use in a wide range of food formulations.

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Functional properties of date powder under ultrasound, microwave and chemical hydrolysis: verifying its quality and safety with FTIR technique

2022

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Seabuckthorn (Hippophae rhamnoides L.), a novel seed protein concentrate: isolation and modification by high power ultrasound and characterization for its functional and structural properties

Cited by 12 publications

References 34 publications

Seabuckthorn seed protein concentrate: a novel seed protein; emulsifying properties as affected by ultrasonication and enzymatic hydrolysis

Seabuckthorn seed protein concentrate: a novel seed protein; emulsifying properties as affected by ultrasonication and enzymatic hydrolysis

Valorization of sea buckthorn seed protein to hydrolysates: Impact on morphological, structural, functional, and antioxidant properties

Functional properties of date powder under ultrasound, microwave and chemical hydrolysis: verifying its quality and safety with FTIR technique

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