Enzyme-induced aggregation and gelation of proteins

Creusot, Nathalie; Gruppen, Harry

doi:10.1016/j.biotechadv.2007.07.007

Cited by 64 publications

(29 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Gelation also depends on disulfide bonds, hydrophobic interactions, and charged groups [11]. Depending on the fact whether hydrolysis is limited or extensive and whether the substrate is native or not, it is assured that different enhancing mechanisms are involved [30]. We found that the denatured SMG suspensions incubated at 50°C in pH 7.0 for 180 min did not form gel, and we got the same results when SMG suspensions were hydrolyzed with trypsin and pepsin (data not shown).…”

Section: Resultssupporting

confidence: 81%

“…On the other hand, upon limited hydrolysis the effective hydrophobicity of certain globular proteins could be increased through exposure of buried apolar residues, resulting in aggregate formation. Creusot and Gruppen [30] have pointed out that the enhancing effect of hydrolysis on protein gelation is a specific property of a hydrolysate, since it is only observed within specific combinations of substrates, enzymes, and degrees of hydrolysis. Gelation also depends on disulfide bonds, hydrophobic interactions, and charged groups [11].…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Functional properties of gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad

Jin

Zhu

et al. 2012

Eur Food Res Technol

View full text Add to dashboard Cite

Gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad (SMG) were obtained by enzymatic hydrolysis using neutrase. Functional properties of SMG hydrolysates (SMGHs) with different degree of hydrolysis (DH: 4.94, 6.84, 7.53 and 11.86%, respectively) were evaluated with the objective to investigate the relations between hydrolysis characteristics and functionalities. The results showed that hydrolysis with neutrase improved the gelation property, solubility, waterholding capacity (WHC), oil-holding capacity (OHC), and surface hydrophobicity (SH), but not foaming capacity (FC) of SMG. The SMGHs at high DH (11.86%) showed better gelation property and solubility than that at low DH (4.94-7.53%). However, the maximum values of WHC, OHC, and SH of SMGHs were found at DH of 4.94%, significantly higher than (p \ 0.05) or equivalent to (p [ 0.05) that of soy protein isolate (SPI) for WHC and OHC. Emulsifying capacity of SMGHs is independent of DH, but restricted by pH environment. The emulsifying activity index of all SMGHs was significantly higher than that of SPI in pH 5 (p \ 0.05) and slightly higher than or equivalent to that of SPI in pH 7. Meanwhile, SMG and SMGHs were abundant in glycine, lysine, alanine, glutamic acid, and aspartic acid, containing all the essential amino acids (41.63-42.90% of the total amino acids). These results imply that SMGHs might be utilized as multifunctional and nutritive ingredients in food industry.

show abstract

Section: Resultssupporting

confidence: 81%

Section: Resultsmentioning

confidence: 99%

Functional properties of gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad

Jin

Zhu

et al. 2012

Eur Food Res Technol

View full text Add to dashboard Cite

show abstract

“…During hydrolysis, some of the soybean protein digests coagulate (Inouye et al, 2002;Nagai & Inouye, 2004) and remain insoluble, resulting in poor solubility. Although characterization has been achieved for these digests (Kuipers et al, 2006;Creusot & Gruppen, 2007;Kuipers et al, 2007;Kuipers et al, 2008), understanding their structure-function relationship is crucial for enhancing the functional properties of soybean proteins (Tsumura et al, 2005b). Enzymatically hydrolytic technology is now in place to improve the physicochemical properties of soybean protein, thereby increasing its value in the market.…”

Section: Resultsmentioning

confidence: 99%

Improvement of the Physicochemical Properties of Soybean Proteins by Enzymatic Hydrolysis

Tsumura

2009

FSTR

View full text Add to dashboard Cite

show abstract

“…Glutamyl endopeptidase can cause hydrolysis of whey proteins and aggregation of generated peptides increases with the degree of hydrolysis. 269 …”

Section: Impuritiesmentioning

confidence: 99%

External Factors Affecting Protein Aggregation

Wang

Speaker

2010

Aggregation of Therapeutic Proteins

View full text Add to dashboard Cite

The behavior of biotherapeutic proteins is signifi cantly different from small molecule drugs both in liquid and solid states, especially in terms of physical stability. One such property is the high tendency of protein molecules to aggregate under a variety of conditions. The aggregation tendency is arguably the most common and troubling manifestation of protein instability during the development of protein biotherapeutics. 1 Protein aggregates usually exhibit either reduced or, in many cases, no biological activity. 2 -5 A clear correlation was established between loss of recombinant factor VIII (rFVIII ) and its degree of aggregation as shown in Fig. 4.1 . 6 To achieve effective prevention or inhibition of protein aggregation, it is of paramount importance to understand all the possible factors that affect or control the protein aggregation process.Many factors have been identifi ed and reported in the literature affecting the process and rate of protein aggregation. These factors can be roughly divided into two major categories: internal (protein structure related) and external (protein environment related). Chapter 3 in this book has focused extensively on factors that belong to the fi rst category. This chapter focuses on the external factors that affect the process and rate of protein aggregation. To facilitate discussion, these external factors are further divided into the following sections: (1) temperature; (2) solution conditions and composition (pH, buffer type and concentration, ionic strength, excipients and level, protein concentration, metal ions, denaturing and reducing agents, impurities, organic solvents, containers/closures, sources of proteins, sample treatment, and analytical methodologies); (3) processing steps (fermentation/expression,

show abstract

Enzyme-induced aggregation and gelation of proteins

Cited by 64 publications

References 10 publications

Functional properties of gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad

Functional properties of gelation-like protein hydrolysates from scallop (Patinopecten yessoensis) male gonad

Improvement of the Physicochemical Properties of Soybean Proteins by Enzymatic Hydrolysis

External Factors Affecting Protein Aggregation

Contact Info

Product

Resources

About