Enhancing the functionality of food proteins by enzymatic modification

Panyam, D.; Kilara, Arun

doi:10.1016/0924-2244(96)10012-1

Cited by 458 publications

(349 citation statements)

References 30 publications

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“…Protein solubilities between 93-98% in the pH range from 3 to 7 were shown for housefly larvae protein after two-step hydrolysis with Alcalase and Flavourzyme (E/S = 2%; t H = 13 h; DH = 60%) by Wang et al [32]. Differences in the extent of solubility increase can be ascribed to the different insect species, pre-treatment, used enzyme(s), E/S ratio, t H , and DH [50]. Table 1) are shown.…”

Section: Protein Solubilitymentioning

confidence: 99%

“…Hall et al [33] have also found improved foamability of banded cricket hydrolysates up to 155% (Alcalase; ES 0.5%, t H = 30 min) in comparison to the control (90%). Similar to phenomena influencing emulsifying properties of MLPF hydrolysates, conformational changes induced by enzymatic cleavage led to the generation of small peptides and exposure of surface-stabilising residues resulting in improved foamability due to rapid diffusion and stabilisation of the interfacial layer [50]. In analogy to the results of the single enzyme hydrolyses, the combination of enzymes resulted in deteriorated foamability of MLPF hydrolysates at neutral and alkaline pH, which might be ascribed to the higher repulsive forces and lower elasticity of the interfacial layer at pH 7-9 in comparison to the isoelectric point around pH 4 [61].…”

Section: Emulsifying and Foaming Propertiesmentioning

confidence: 99%

“…Various parameters such as type, activity, and concentration of the enzyme(s), initial degree of nativity/denaturation of the protein, milieu conditions (T, pH, ionic strength) and hydrolysis time (t H ) affect the proteolysis and consequently the resulting DH value [50]. The DH of the MLPF was continuously monitored during the different enzymatic hydrolyses ( Table 2).…”

Section: Degree Of Hydrolysis (Dh)mentioning

confidence: 99%

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Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Purschke

Meinlschmidt

Horn

et al. 2017

Eur Food Res Technol

106

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Enzymatic hydrolysis of migratory locust (Locusta migratoria L.) protein flour (MLPF) was investigated as a method to improve the techno-functional properties. Experiments were conducted under variation of the applied proteases (Alcalase, Neutrase, Flavourzyme, Papain) or combinations thereof, enzyme-substrate ratio (0.05-1.0% w/w), heat pre-treatment (60-80 °C; 15-60 min), and hydrolysis time (0-24 h). Protein degradation was monitored in terms of degree of hydrolysis (DH) and SDS-PAGE. Solubility, emulsifying, foaming and water/oil binding properties of the hydrolysates were determined. In comparison to the control (DH = 5%), hydrolysis resulted in considerably higher DH values up to 42%. SDS-PAGE profiles revealed a steady decrease of bands between 25 and 75 kDa and an increase of low molecular weight bands (10-15 kDa). However, different heat pre-treatments resulted in impaired hydrolytic cleavage as evidenced by lower DH values. Protein solubility of MLPF hydrolysates was improved over a broad pH range from initially 10-22% up to 55% at alkaline conditions. Furthermore, hydrolysis resulted in enhanced emulsifying activity (54%) at pH 7, improved foamability (326%) at pH 3 and advanced oil binding capacity. The results of this study have clearly demonstrated the potential of targeted enzymatic degradation to improve the techno-functionality of migratory locust protein in order to produce tailored insect-based ingredients for the use in food applications.

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Section: Protein Solubilitymentioning

confidence: 99%

Section: Emulsifying and Foaming Propertiesmentioning

confidence: 99%

Section: Degree Of Hydrolysis (Dh)mentioning

confidence: 99%

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Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Purschke

Meinlschmidt

Horn

et al. 2017

Eur Food Res Technol

106

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“…DH close to 100% means that all proteins in the sample are completely hydrolyzed to free amino acids (Panyam & Kilara, 1996). As shown in Table 1, DH of KA and KM was 15.93 and 13.23%, respectively.…”

Section: Degree Of Hydrolysis (Dh)mentioning

confidence: 79%

Untitled

Pongsetkul¹,

Benjakul²,

Sumpavapol³

et al. 2017

Turk. J. Fish. Aquat. Sci.

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Autolysis of Acetes vulgaris and Macrobrachium lanchesteri was comparatively studied. Maximal autolytic activities were found at pH 7, 55°C for A. vulgaris and pH 8, 60°C for M. lanchesteri. Both shrimps dominantly contained serine proteases as indicated by the marked inhibition by PMSF and SBTI. When both shrimps were used for Kapi production and characterized, differences in characteristics as well as antioxidant activities were obtained. Kapi produced from A. vulgaris (KA) showed the higher degree of hydrolysis (15.93±0.51%), peroxide values (0.20±0.23 mg cumene peroxide/ kg sample) and TBARS value (0.55±0.16 mg MDA/ kg sample), compared with Kapi produced from M. lanchesteri (KM), indicating the higher protein degradation and lipid oxidation in this sample. Moreover, KA also possessed the higher antioxidative activities including ferric reducing antioxidant power (FRAP) (14.12±1.34 µmol TE/ g sample), chelating activity (3.21±0.05 µmol EE/ g sample), hydrogen peroxide (30.05±0.49 µmol TE/ g sample) and singlet oxygen scavenging activities (48.46±0.32 µmol EE/ g sample) than KM, except for DPPH and ABTS radical scavenging activities, which showed lower activity (P<0.05) and had no difference (P>0.05), respectively. Therefore, different levels and types of endogenous proteases in both shrimps determined the autolysis, characteristics and antioxidative properties of resulting Kapi.

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“…This complicates their utilization in foodstuffs of moderate acidity, such as citric beverages and dressings, especially when the required functional properties depend on solubility (WalStra, 1989). In this regard, partial hydrolysis of proteins with proteases is used to improve their functional properties, particularly solubility over a wide pH range (PanyaM & kilara, 1996). There is an increasing demand for protein hydrolysates for commercial applications, like a number of formulated diets that are suitable for geriatrics, high-energy supplements or hypoallergenic infant formulas.…”

mentioning

confidence: 99%

Effects of increasing acylation and enzymatic hydrolysis on functional properties of bambara bean (Vigna subterranea) protein concentrate

Muné¹,

Minka²,

Mbome³

2014

Acta Alimentaria

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Bambara bean protein concentrate was acylated and partially hydrolysed with pancreatin in order to improve its functional properties. Increasing acetylation and succinylation (from 0.0 to 1.0 g anhydride/g concentrate) modified lysine at similar rate. Acylation markedly improved protein solubility and water solubility index at neutral pH, which reached to 92 and 94%, respectively. Acetylation showed greater effect on emulsifying activity, which was maximum at 0.5 g anhydride/g concentrate, and emulsifying stability was higher at 0.25 g anhydride/g concentrate. A significant increase in foam capacity was recorded at 0.5 g succinic anhydride/g concentrate, and foam stability decreased detrimentally following acylation. Fat absorption capacity was not improved by acylation. At pH 3.5, protein solubility of acylated concentrate was low (<14%). Hydrolysis of protein concentrate with pancreatin resulted in significant increase in protein solubility at neutral pH. At isoelectric pH, solubility of protein hydrolysates increased with the increasing degree of hydrolysis.

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Enhancing the functionality of food proteins by enzymatic modification

Cited by 458 publications

References 30 publications

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

Improvement of techno-functional properties of edible insect protein from migratory locust by enzymatic hydrolysis

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Effects of increasing acylation and enzymatic hydrolysis on functional properties of bambara bean (Vigna subterranea) protein concentrate

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