Partially hydrolyzed rapeseed protein isolates with improved functional properties

Vioque, Javier; Sánchez‐Vioque, Raúl; Clemente, Alfonso; Pedroche, Josto; Millán, Francisco

doi:10.1007/s11746-000-0072-y

Cited by 185 publications

(149 citation statements)

References 13 publications

(15 reference statements)

Supporting

Mentioning

131

Contrasting

Unclassified

Order By: Relevance

“…Another source of proteins can be used as substrate for enzyme hydrolysis too. Parrado et al [1] and Villanueva et al [2] have obtained sunflower protein hydrolysates from sunflower seed protein isolates, Vioque et al [3] have produced rape seed protein hydrolysates.…”

Section: Introductionmentioning

confidence: 99%

Composition and properties of partially hydrolyzed sunflower protein isolates

Nosenko¹,

Mank²,

Zhukova³

et al. 2016

Ukr. food j.

View full text Add to dashboard Cite

Introduction. Partial enzyme hydrolysis of proteins is common method of modification of their functional properties. The characteristics of partially hydrolyzed proteins obtained from sunflower meal are presented in this work.Materials and methods. Proteins of sunflower meal were extracted in the presence of two proteases viz. neutral protease and Alkalase during 40 min. Partially hydrolyzed protein samples were prepared by isoelectric precipitation and next drying. The polypeptide composition of protein isolates were studied by polyacrylamide gel electrophoresis, degree of protein hydrolysis, amino acid composition, surface activity and functional properties were estimated.Results and discussion. The polypeptides of higher molecular weight (45-54 and about 32-35 kDa) were absent in polypeptide profile of partially hydrolyzed proteins either of proteases. At the same time they were abounded with 14-16 kDa polypeptides and polypeptides with molecular weight lower 14 kDa.Partially hydrolyzed protein samples had higher protein content, lower content of ash and carbohydrates as compared with the control sample. The biological value of sunflower protein isolates were limited by three amino acids -sulfur containing amino acids (methionine and cysteine) and lysine. The content of methionine, cysteine and lysine has been increased in protein samples obtained with neutral protease, relative to protein isolate. Differential scanning calorimetric analyze of protein samples have demonstrated that partially hydrolyzed samples contained undenaturated proteins, but their denaturation degree was higher compared with control samples. Partial hydrolysis of sunflower seed proteins have improved their solubility in pH range from 2 to 8, water holding, oil binding, foaming, emulsifying capacities and surface activity.Conclusions. Partially hydrolyzed protein samples had higher protein content, lighter color, lower degree of denaturation and better functional properties compared to the traditional protein isolates.

show abstract

Section: Introductionmentioning

confidence: 99%

Composition and properties of partially hydrolyzed sunflower protein isolates

Nosenko¹,

Mank²,

Zhukova³

et al. 2016

Ukr. food j.

View full text Add to dashboard Cite

show abstract

“…Protein hydrolysates with different degrees of hydrolysis can be used as flavorings in soups, sauces, and meat products (Weir, 1986). Protein hydrolysates most likely have improved functional properties compared to the original proteins and are commonly used as food ingredients (Vioque et al, 2000). In medical field, protein hydrolysates are widely used as diet supplements or hypoallergenic foods (Frokjear, 1994).…”

Section: Introductionmentioning

confidence: 99%

Nutritional and functional properties of Roselle (Hibiscus sabdariffa L.) seed protein hydrolysates

Tounkara

Sodio

Chamba

et al. 2014

Emir. J. Food Agric

View full text Add to dashboard Cite

The nutritional and functional properties of Roselle seed protein hydrolysates (RSPH) were studied. Roselle seed protein isolates were digested (for 1.5 h and 3h) using pepsin followed by pancreatin. The maximum nitrogen solubility values of 94.17 and 90.8 were observed at pH 12 and pH 10 after 1.5 h and 3 h of hydrolysis, respectively. RSPH1.5 and RSPH3 exhibited a good foaming capacity of 310 and 300% respectively. Furthermore, RSPH1.5 showed the best foaming stability (300%) after 60 min compared to RSPH3 (144%) at the same time. For both hydrolysates, the amounts of essential amino acids exceeded those recommended by the Food and Agricultural Organization/World Health Organization (2007) for humans. The emulsifying capacity of RSPH1.5 was higher than that of RSPH3 90 and 100 mL/g respectively. RSPH1.5 possessed also the highest water holding and oil holding capacities compared to RSPH3. RSPH3 was more heat sensitive than RSPH1.5. The denaturation temperature for RSPH1.5 and RSPH3 were 95.80ºC and 85.93ºC respectively. Our results demonstrated that RSPH may be used wholly or partially to replace high-price materials like egg albumen and casein as well as a potential food ingredient.

show abstract

“…Proteolytic enzyme modification of proteins is an effective way to improve the various functional properties and to increase the field of application of the proteins [8][9][10] . The peptides that are produced by partial hydrolysis of proteins have smaller molecular size and less secondary structure than the original proteins.…”

Section: Introductionmentioning

confidence: 99%

Preparation and Characterisation of Protein Hydrolysates from Indian Defatted Rice Bran Meal

Bandyopadhyay¹,

Misra

Ghosh

2008

J. Oleo Sci.

View full text Add to dashboard Cite

Rice bran meal is a very good source of protein along with other micronutrients. Rice bran meal has been utilized to produce protein isolates and respective protein hydrolysates for potential application in various food products. De-oiled rice bran meal, available from Indian rice bran oil extraction plants, was initially screened by passing through an 80-mesh sieve (yield about 70%). A fraction (yield-30%) rich in fibre and silica was initially discarded from the meal. The protein content of the through fraction increased from 20.8% to 24.1% whereas silica content reduced from 3.1% to 0.4%. Rice bran protein isolate (RPI) was prepared by alkaline extraction followed by acidic precipitation at isoelectric point. This protein isolate was hydrolysed by papain at pH 8.0 and at 37 for 10, 20, 30, 45 and 60 minutes. The peptides produced by partial hydrolysis had been evaluated by determining protein solubility, emulsion activity index (EAI), emulsion stability index (ESI), foam capacity and foam stability (FS). All protein hydrolysates showed better functional properties than the original protein isolate. These improved functional properties of rice bran protein hydrolysates would make it useful for various application especially in food, pharmaceutical and related industries.

show abstract

Partially hydrolyzed rapeseed protein isolates with improved functional properties

Cited by 185 publications

References 13 publications

Composition and properties of partially hydrolyzed sunflower protein isolates

Composition and properties of partially hydrolyzed sunflower protein isolates

Nutritional and functional properties of Roselle (Hibiscus sabdariffa L.) seed protein hydrolysates

Preparation and Characterisation of Protein Hydrolysates from Indian Defatted Rice Bran Meal

Contact Info

Product

Resources

About