Correlation between the Degree of Hydrolysis and the Peptide Profile of Whey Protein Concentrate Hydrolysates: Effect of the Enzyme Type and Reaction Time

Morais, Harriman Aley; Silve, Marialice P.C.; Silva, Viviane D. M.; Silva, Mauro R.; S, Ana Cristina; Silveir, Josianne N.

doi:10.3923/ajft.2013.1.16

Cited by 33 publications

(13 citation statements)

References 22 publications

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“…On the other hand, hydrolysis by B . licheniformis proteases, such as Prolyve, is expected to release peptides without free amino acids [ 49 ]. Debitrase hydrolysates had a higher proportion of components with lower molecular mass (<1 kDa) compared to Prolyve hydrolysates, e.g., in the case of NaCN (56% versus 49%) and WPC (43.5% versus 40%).…”

Section: Resultsmentioning

confidence: 99%

Impact of Enzymatic Hydrolysis and Heat Inactivation on the Physicochemical Properties of Milk Protein Hydrolysates

Gruppi

Dermiki

Spigno

et al. 2022

Foods

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This study determined the physicochemical properties (apparent viscosity (ηapp), turbidity (A550nm), particle size and molecular mass distribution) of hydrolysates generated from whey protein concentrate (WPC), milk protein concentrate (MPC) and sodium caseinate (NaCN), following incubation with Debitrase HYW20™ and Prolyve™ at 50 °C, pH 7.0 for 1 and 4 h, before and after heat inactivation (80 °C for 10 min). The degree of hydrolysis (DH) increased with incubation time, giving values of 6.56%, 8.17% and 9.48%, following 1 h hydrolysis of WPC, MPC and NaCN with Debitrase HYW20™, and 12.04%, 15.74% and 17.78%, respectively, following 4 h incubation. These DHs were significantly higher compared to those obtained following 4 h incubation with Prolyve™. Hydrolysis with Debitrase HYW20™ gave >40% of peptides with molecular masses < 1 kDa for all substrates, which was higher than the value obtained following hydrolysis with Prolyve™. The effect of hydrolysis on the physicochemical properties was substrate dependent, since ηapp decreased in WPC and NaCN hydrolysates, particle size decreased for all the substrates, with aggregate formation for MPC, and turbidity decreased in WPC and MPC hydrolysates, while it increased in NaCN hydrolysates. The physical properties of the hydrolysates were influenced by the enzyme thermal inactivation step in a DH-dependent manner, with no significant effect on turbidity and viscosity for hydrolysates at higher DHs.

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Section: Resultsmentioning

confidence: 99%

Impact of Enzymatic Hydrolysis and Heat Inactivation on the Physicochemical Properties of Milk Protein Hydrolysates

Gruppi

Dermiki

Spigno

et al. 2022

Foods

View full text Add to dashboard Cite

show abstract

“…Degree of hydrolysis (DH) was calculated using soluble protein content method (Morais et al, 2013;Sinha and Khare, 2015). One milliliter of 10% (w/v) trichloroacetic acid was added to 1 ml of the aliquot collected after enzymatic hydrolysis and incubated at 37 • C for 30 min.…”

Section: Whey Protein Hydrolysismentioning

confidence: 99%

Cloning, Expression, and Structural Elucidation of a Biotechnologically Potential Alkaline Serine Protease From a Newly Isolated Haloalkaliphilic Bacillus lehensis JO-26

Bhatt

Singh

2020

Front. Microbiol.

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An alkaline protease gene of Bacillus lehensis JO-26 from saline desert, Little Rann of Kutch, was cloned and expressed in Escherichia coli BL21 (DE3). A 1,014-bp ORF encoded 337 amino acids. The recombinant protease (APrBL) with Asp 97, His 127, and Ser 280 forming catalytic triad belongs to the subtilase S8 protease family. The gene was optimally expressed in soluble fraction with 0.2 mM isopropyl β-D-thiogalactopyranoside (IPTG), 2% (w/v) NaCl at 28 • C. APrBL, a monomer with a molecular mass of 34.6 kDa was active over pH 8-11 and 30 • C−70 • C, optimally at pH 10 and 50 • C. The enzyme was highly thermostable and retained 73% of the residual activity at 80 • C up to 3 h. It was significantly stimulated by sodium dodecyl sulfate (SDS), Ca 2+ , chloroform, toluene, n-butanol, and benzene while completely inhibited by phenylmethylsulfonyl fluoride (PMSF) and Hg 2+ . The serine nature of the protease was confirmed by its strong inhibition by PMSF. The APrBL gene was phylogenetically close to alkaline elastase YaB (P20724) and was distinct from the well-known commercial proteases subtilisin Carlsberg (CAB56500) and subtilisin BPN (P00782). The structural elucidation revealed 31.75% α-helices, 22.55% β-strands, and 45.70% coils. Although high glycine and fewer proline residues are a characteristic feature of the cold-adapted enzymes, the similar observation in thermally active APrBL suggests that this feature cannot be solely responsible for thermo/cold adaptation. The APrBL protease was highly effective as a detergent additive and in whey protein hydrolysis.

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“…The gelatin hydrolysate was then dried by the freezing-drying method. The DH of gelatin hydrolysate was detected based on the quantification of the soluble protein [ 50 ]. The SDS-PAGE analysis of gelatin hydrolysate was according to the SDS-PAGE protocol described above.…”

Section: Methodsmentioning

confidence: 99%

Utilization of Seafood Processing By-Products for Production of Proteases by Paenibacillus sp. TKU052 and Their Application in Biopeptides’ Preparation

et al. 2020

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Microbial fermentation of by-products is a renewable and efficient technique in the development of a range of useful products. In this study, protease synthesis by Paenibacillus sp. TKU052 was carried out on culture media containing some common seafood processing by-products (SPBPs) as the sole source of carbon and nitrogen (C/N). The most suitable C/N nutrition source for the production of proteases was found to be 3.0% (w/v) demineralized crab shells powder (deCSP) and maximal enzyme activity of 4.41 ± 0.16 U/mL was detected on the third day of the culture. Two proteases (P1 and P2) with a similar molecular weight of 31 kDa were successfully isolated and purified from the 3-day deCSP-containing medium. Both P1 and P2 exhibited the highest activity of gelatin hydrolysis at pH 6 and 60 °C. The gelatin hydrolysates catalyzed by Paenibacillus TKU052 proteases were evaluated for biological activities, including 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging, angiotensin-I converting enzyme (ACE) inhibition, and prebiotic activities. The gelatin hydrolysates expressed 31.76–43.95% DPPH radical scavenging activity and 31.58–36.84% ACE inhibitory activity, which was higher than those from gelatin. Gelatin hydrolysates also showed the growth-enhancing effect on Bifidobacterium bifidum BCRC 14615 with an increase to 135.70–147.81%. In short, Paenibacillus sp. TKU052 could be a potential strain to utilize crab shell wastes to produce proteases for bio-active peptides’ preparation.

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Correlation between the Degree of Hydrolysis and the Peptide Profile of Whey Protein Concentrate Hydrolysates: Effect of the Enzyme Type and Reaction Time

Cited by 33 publications

References 22 publications

Impact of Enzymatic Hydrolysis and Heat Inactivation on the Physicochemical Properties of Milk Protein Hydrolysates

Impact of Enzymatic Hydrolysis and Heat Inactivation on the Physicochemical Properties of Milk Protein Hydrolysates

Cloning, Expression, and Structural Elucidation of a Biotechnologically Potential Alkaline Serine Protease From a Newly Isolated Haloalkaliphilic Bacillus lehensis JO-26

Utilization of Seafood Processing By-Products for Production of Proteases by Paenibacillus sp. TKU052 and Their Application in Biopeptides’ Preparation

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