Proteins: General

Pomeranz, Y.

doi:10.1016/b978-0-12-561280-7.50009-7

Cited by 6 publications

(1 citation statement)

References 13 publications

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“…The most important functional property of proteins is the solubility, such that loss of solubility has been used as an indication for loss of functionality. Generally, superior functional attributes for most applications in food processing are directly related to the solubility of proteins (8,9).…”

Section: Introductionmentioning

confidence: 99%

Functional Properties of Guava Seed Glutelins

Bernardino-Nicanor

Añón

Scilingo

et al. 2005

J. Agric. Food Chem.

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Five guava seed glutelin extracts were obtained with different buffer solutions: Na(2)B(4)O(7) alone (Glut.Bo) or containing SDS (Glut. BoSDS), 2-mercaptoethanol (Glut.Bo2-ME), or a combination of both (Glut. BoSDS2-ME) and NaOH (Glut.Na). All borate buffer solutions were at pH 10. The higher yield of glutelins corresponded to the Glut. BoSDS extract (81.9% dry basis) and the lower to Glut.Bo (6.8%). The functional properties of the five guava seed glutelin extracts were determined. Glut. BoSDS, Glut. BoSDS2-ME, and Glut.Na showed high values for several properties, including surface hydrophobicity (7.7, 10.8, and 0.6, respectively), solubility at pH 10 (91.1, 77.9, and 96.7, respectively), water-holding capacity at pH 3.6 (1.7, 2.5, and 2.8, respectively), emulsifying activity index (pH 10; 503.5, 238.2, and 838.0, respectively), and foaming properties (pH 10; V(0) = 0.14, 0.25, and 0.19, respectively; V(max) = 6.1, 5.59, and 4.51, respectively; t(1/2) = 266, 255.3, and 94 s, respectively). These results suggest that the denaturing reagent (SDS or NaOH) during extraction conferred on the proteins a structure that facilitated the development of their functional properties.

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Section: Introductionmentioning

confidence: 99%

Functional Properties of Guava Seed Glutelins

Bernardino-Nicanor

Añón

Scilingo

et al. 2005

J. Agric. Food Chem.

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Alkali‐modified soy protein with improved adhesive and hydrophobic properties

Hettiarachchy

Kalapathy

Myers

1995

J Americ Oil Chem Soc

236

158

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Adhesive and hydrophobic properties of alkalimodified soy protein (AMSP) and trypsin-modified soy protein (TMSP) on wood were investigated. Modifying soy protein (i) under moderate alkaline conditions (pH 10.0 at 50°C) and (ii) with trypsin, enhanced adhesive strengths (730 and 743 N, respectively) compared with unmodified soy protein (340 N). Hydrophobicities of AMSP, TMSP, and unmodified soy protein isolate by sodium dodecyl sulfate binding and 1-anilino-8-naphthatene sulfonate methods were 7.6, 6.4, 5.0 and 39, 27, 13, respectively. Modified soy protein adhesives with higher hydrophobicities (AMSP and TMSP) had enhanced water-resistance properties.alone may not yield optimal results, combination treatments of alkaline pH coupled with a moderate temperature were explored.Water resistance is an important glue property that determines adhesive bond durability (11). To improve water resistance of soy protein glue, several cross-linking agents, such as calcium salts and carbon disulfide, have been used (11). Adhesives prepared from soy meal have poor water resistance due to the presence of carbohydrates (1 t). Improved adhesive strength and water resistance have been observed in glue prepared from trypsin-modified soy protein (TMSP) (13). Since limited information is available on the adhesive and water-resistance properties of soy protein isolates (SPI) modified by combinations of alkali and heat treatments, we investigated the effects of these treatments.Preparation of modified protein: TMSP. TMSP was prepared according to the method described by Kalapathy et aL (13). A 7% solution of SPI with trypsin (E/S = 1:50, pH 8.0) was incubated at 37°C for 1 h in a shaker (180 rpm). The enzyme was inactivated by heating at 90°C for 3 min, and the product was frozen and freeze-dried~ Degree of hydrolysis. Degree of hydrolysis was determined by measuring insoluble nitrogen in 10% trichloro

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Physicochemical properties of pronase‐treated rice glutelin

Anderson

Hettiarachchy

2001

J Americ Oil Chem Soc

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Rice glutelin protein was extracted from defatted medium-grain rice by alkali extraction followed by acid precipitation. Extracted glutelin was hydrolyzed with Pronase E, a bacterial protease, and the functional properties of hydrolysates were evaluated. Nitrogen solubility of pronase-treated glutelin protein increased from pH 2 to pH 12. Similarly, foaming and emulsion properties of hydrolyzed protein also showed improved characteristics. The emulsion activity, expressed as the turbidity of diluted emulsions, was significantly greater (P ≤ 0.05) for hydrolyzed samples. However, turbidity for all samples decreased with increased homogenization time, indicating a decrease in the volume of dispersed oil. There were significant changes in apparent viscosity as a function of shear rate, with viscosity decreasing with increasing shear rate. The viscosity of dispersions of all hydrolyzed samples was significantly lower than that of the native sample at all shear rates tested. Enzymatic hydrolysis of rice endosperm storage glutelin proteins appeared to improve the functional characteristics of the hydrolyzed proteins.

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Proteins: General

Cited by 6 publications

References 13 publications

Functional Properties of Guava Seed Glutelins

Functional Properties of Guava Seed Glutelins

Alkali‐modified soy protein with improved adhesive and hydrophobic properties

Physicochemical properties of pronase‐treated rice glutelin

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