Effects of heat and proteolysis on deamidation of food proteins using peptidoglutaminase

Hamada, Jamel S.

doi:10.1021/jf00017a003

Cited by 45 publications

(30 citation statements)

References 12 publications

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“…Gill et al (8) reported that peptidoglutaminases are not active against caseins and whey proteins even after denaturation and are only active against glutaminyl residues in peptides with a molecular weight below 5,000. Hamada (9) reported slight enhancements of peptidoglutaminase-catalyzed protein deamidation using heat-and/or alkaline-treated proteins, but the degrees of deamidation were very low (0.8 to 3.0% for caseins) compared to those for the preparations treated by the combinations with proteolysis (ca. 38%).…”

Section: Discussionmentioning

confidence: 98%

A Novel Protein-Deamidating Enzyme from Chryseobacterium proteolyticum sp. nov., a Newly Isolated Bacterium from Soil

Yamaguchi¹,

Yokoe²

2000

Appl Environ Microbiol

149

146

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A novel protein-deamidating enzyme, which has potential for industrial applications, was purified from the culture supernatant of Chryseobacterium proteolyticum strain 9670 T isolated from rice field soil in Tsukuba, Japan. The deamidating activities on carboxybenzoxy (Cbz)-Gln-Gly and caseins and protease activity were produced synchronously by the isolate. Both deamidating activities were eluted as identical peaks separated from several proteases by phenyl-Sepharose chromatography of the culture supernatant. The enzyme catalyzed the deamidation of native caseins with no protease and transglutaminase activities. Phenotypic characterization and DNA analyses of the isolate were performed to determine its taxonomy. Physiological and biochemical characteristics, 16S rRNA gene sequence analysis, and DNA-DNA relatedness data indicated that the isolate should be placed as a new species belonging to the genus Chryseobacterium. The isolate showed no growth on MacConkey agar and produced acid from sucrose. The levels of DNA-DNA relatedness between the isolate and other related strains were less than 17%. The name Chryseobacterium proteolyticum is proposed for the new species; strain 9670 is the type strain (‫؍‬FERM P-17664).An enzyme catalyzing deamidation of proteins has a great potential for industrial applications. Deamidation of proteins can improve protein functionalities such as solubility, emulsification, and foaming and gelation properties, which are desired properties in some food proteins. Most plant proteins have poor solubility and functionality under mild acidic conditions, which are the pH ranges of most food systems, resulting in their limited use in foods. Because the contents of glutamine residue in plant proteins are generally high, deamidation of such proteins is one of the most promising ways to expand their uses and to improve their functionalities. Many studies of the chemical (mild acid or alkaline treatment) or physical (dry heat treatment) deamidation of food proteins had reported and demonstrated the effectiveness of deamidation for improvement of protein functionalities (see reference 25 for review). To avoid unfavorable side effects brought about by nonenzymatic treatments-for example, concomitant peptide bond cleavage, off-flavor formation, and amino acid racemization-enzymatic deamidations of proteins have been examined (see reference 10 for review). Protease (16), transglutaminase (23), and peptidoglutaminase (9) were used for this purpose. None of their primary reactions were deamidations, or the enzymic substrates were peptides rather than proteins. Besides the improvement in protein functionalities, protein-deamidating enzymes could be used for many applications, including protein structure analysis.In 1971, Kikuchi et al. (17) found an enzyme, peptidoglutaminase, from Bacillus circulans that deamidates the peptidebound glutamines. This enzyme was not active on high-molecular-weight peptides, i.e., proteins such as caseins, unless the proteins were hydrolyzed to short peptides (17). In p...

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Section: Discussionmentioning

confidence: 98%

A Novel Protein-Deamidating Enzyme from Chryseobacterium proteolyticum sp. nov., a Newly Isolated Bacterium from Soil

Yamaguchi¹,

Yokoe²

2000

Appl Environ Microbiol

149

146

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“…Enzymatic methods using transglutaminase (TG) (Motoki, Seguro, Nio, & Takinami, 1986;Nonaka, Sawa, Matsuura, Motoki, & Nio, 1996;Ohtsuka, Umezawa, Nio, & Kubota, 2006), peptide-glutaminase (Hamada & Marshall, 1989, 1992, a combination of pH and protease (Matsudomi, Tanaka, Kato, & Kobayashi, 1986) and protein-glutaminase (PG) are known to be useful for the deamidation of food proteins.…”

Section: Introductionmentioning

confidence: 99%

“…Additionally, Hamada and Marshall (1992) reported that heat and proteolysis in casein deamidation using peptide-glutaminase and partial protein hydrolysis prior to enzymatic treatment increase the deamidation of casein amide residues. Previous research on the basic characteristics of PG has demonstrated that alpha-and beta-casein are excellent substrates of PG , and Gu et al (2001) reported that the molten globule state of alpha-lactalbumin, a milk whey proteins, affects the reactivity of PG.…”

Section: Introductionmentioning

confidence: 99%

Effect of deamidation by protein-glutaminase on physicochemical and functional properties of skim milk

Miwa

Yokoyama

Wakabayashi

et al. 2010

International Dairy Journal

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“…Deamidation of proteins can improve their solubility, emulsifying activity, foaming activity, and other functional properties by increasing the number of negative charges and changing the overall structure (9). The chemical methods for protein deamidation, which include acid treatment, anion-catalyzed deamidation, dry heating under alkaline conditions, and thermal treatment, all cause collateral peptide bond cleavages (10,11).…”

mentioning

confidence: 99%

Crystal Structures of Protein Glutaminase and Its Pro Forms Converted into Enzyme-Substrate Complex

Hashizume

Maki

Mizutani

et al. 2011

Journal of Biological Chemistry

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Background: Protein glutaminase (PG) catalyzes deamination of Gln residues in proteins. Results: The structures of mature and pro forms and a pro form mutant reveal that the side chain of Gln-47 of mutant A47Q mimics the protein substrate of PG. Conclusion: Gln-47 of A47Q forms an S-acyl covalent intermediate with the catalytic Cys. Significance: PG shares a common catalytic mechanism with transglutaminase and cysteine protease.

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Effects of heat and proteolysis on deamidation of food proteins using peptidoglutaminase

Cited by 45 publications

References 12 publications

A Novel Protein-Deamidating Enzyme from Chryseobacterium proteolyticum sp. nov., a Newly Isolated Bacterium from Soil

A Novel Protein-Deamidating Enzyme from Chryseobacterium proteolyticum sp. nov., a Newly Isolated Bacterium from Soil

Effect of deamidation by protein-glutaminase on physicochemical and functional properties of skim milk

Crystal Structures of Protein Glutaminase and Its Pro Forms Converted into Enzyme-Substrate Complex

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