Functional properties of proteolytic enzyme modified soy protein isolate

Kim, Sook Y.; Park, Peter S. W.; Rhee, K. C.

doi:10.1021/jf00093a014

Cited by 197 publications

(127 citation statements)

References 17 publications

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“…After the reaction, reactant was conducted by glass filter. Degree of hydrolysis (DH) was determined by measuring the soluble nitrogen content in 10% trichloroacetic acid as followed by Kim et al (1990), and lyophilized hydrolysates were stored at -80°C until use.…”

Section: Preparation Of Rainbow Trout Muscle Hydrolysatementioning

confidence: 99%

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

Kim¹,

Byun

2012

Fisheries and aquatic sciences

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The purpose of this study was the purification and characterization of an angiotensin I converting enzyme (ACE) inhibitory peptide purified from enzymatic hydrolysates of rainbow trout Oncorhynchus mykiss muscle. After removal of lipid, the approximate composition analysis of the rainbow trout revealed 24.4%, 1.7%, and 68.3% for protein, lipid, and moisture, respectively. Among six hydrolysates, the peptic hydrolysate exhibited the highest ACE inhibitory activity. We attempted to purify ACE inhibitory peptides from peptic hydrolysate using high performance liquid chromatography on an ODS column. The IC 50 value of purified ACE inhibitory peptide was 63.9 μM. The amino acid sequence of the peptide was identified as Lys-Val-Asn-Gly-Pro-Ala-Met-SerPro-Asn-Ala-Asn, with a molecular weight of 1,220 Da, and the Lineweaver-Burk plots suggested that they act as a competitive inhibitor against ACE. Our study suggested that novel ACE inhibitory peptides purified from rainbow trout muscle protein may be beneficial as anti-hypertension compounds in functional foods.

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Section: Preparation Of Rainbow Trout Muscle Hydrolysatementioning

confidence: 99%

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

Kim¹,

Byun

2012

Fisheries and aquatic sciences

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“…Many studies have demonstrated that the enzymatic hydrolysis of soybean proteins improved its functional properties, including solubility, emulsification and foaming characteristics (Puski, 1975;Zakaria & McFeeters, 1978;Gunther, 1979;Kamata et al, 1984;Kim et al, 1990;Qi et al, 1997;Were et al, 1997;MolinaOrtiz & Wanger, 2002;Ruíz-Henestrosa et al, 2007). Glycinin and β-conglycinin, the major components of soybean protein, are linked to the functional properties of soybean proteins (Nielsen, 1985;Utsumi et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Improvement of the Physicochemical Properties of Soybean Proteins by Enzymatic Hydrolysis

Tsumura

2009

FSTR

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“…The peptides that are produced by partial hydrolysis of proteins have smaller molecular size and less secondary structure than the original proteins. The protein solubility, emulsifying properties and foaming properties can be improved with a limited degree of hydrolysis [11][12][13] , whereas excessive hydrolysis often causes loss of some of these functionalities 14) . Protein hydrolysates are widely used as nutritional supplements, functional ingredients and flavour enhancers in foods, coffee whiteners, cosmetics, personal care products, and confectionery, and in the fortification of soft drinks and juices.…”

Section: Introductionmentioning

confidence: 99%

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

Bandyopadhyay¹,

Misra

Ghosh

2008

J. Oleo Sci.

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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.

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Functional properties of proteolytic enzyme modified soy protein isolate

Cited by 197 publications

References 17 publications

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

The Novel Angiotensin I Converting Enzyme Inhibitory Peptide from Rainbow Trout Muscle Hydrolysate

Improvement of the Physicochemical Properties of Soybean Proteins by Enzymatic Hydrolysis

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

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