Controlled Hydrolysis of Cheese Whey Proteins Using Trypsin and α-Chymotrypsin

Galvão, Célia M.A.; Silva, Astréa F. Souza; Custódio, Marcos Franqui; Giordano, Raquel de Lima Camargo

doi:10.1007/978-1-4612-0217-2_64

Cited by 12 publications

(14 citation statements)

References 13 publications

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“…This fact was confirmed when the maximum degree of hydrolysis of ''frescal" cheese whey by two endoproteases was measured: 12.1% of the peptide links for trypsin and 19.5% for chymotrypsin (Galvão et al, 2001). When the whey proteins were sequentially hydrolyzed with trypsin and chymotrypsin, however, the total DH was 28.6% and not 31.6% (12.1 + 19.5%).…”

Section: Kinetic Fitting Tools and Statistical Analysismentioning

confidence: 84%

Producing a phenylalanine-free pool of peptides after tailored enzymatic hydrolyses of cheese whey

Galvão

Pinto

Jesus

et al. 2009

Journal of Food Engineering

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Section: Kinetic Fitting Tools and Statistical Analysismentioning

confidence: 84%

Producing a phenylalanine-free pool of peptides after tailored enzymatic hydrolyses of cheese whey

Galvão

Pinto

Jesus

et al. 2009

Journal of Food Engineering

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“…The optimal temperature and pH for the performance of trypsin are 37°C and pH 7.8 (Olsen et al, 2004). At 55°C, it was observed that trypsin activity decreased quickly (Galvão, Silva, Custódio, Monti, & Giordano, 2001). At low temperature, its denaturing is slow.…”

Section: Introductionmentioning

confidence: 97%

Hydrolysis of β-lactoglobulin by trypsin under acidic pH and analysis of the hydrolysates with MALDI–TOF–MS/MS

et al. 2011

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“…It contains 93-94% water, 4.5-5% lactose, 0.8-1% total protein, 0.5-0.7% minerals, and others. 13 Whey accounts for 90% of the initial milk volume processed, which means that approximately 9 L of whey are produced from 10 L of bovine milk during cheese-making. Whey worldwide production is estimated to be 190,000,000 ton/ year.…”

Section: Introductionmentioning

confidence: 99%

Characterizing the release of bioactiveN-glycans from dairy products by a novel endo-β-N-acetylglucosaminidase

Karav¹,

Bell²,

Parc³

et al. 2015

Biotechnol Progress

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Endo-β-N-acetylglucosaminidase isolated from B. infantis ATCC 15697 (EndoBI-1) is a novel enzyme that cleaves N-N′-diacetyl chitobiose moieties found in the N-glycan core of high mannose, hybrid, and complex N-glycans. These conjugated N-glycans are recently shown as a new prebiotic source that stimulates the growth of a key infant gut microbe, Bifi-dobacterium longum subsp. Infantis. The effects of pH (4.45–8.45), temperature (27.5–77.5°C), reaction time (15–475 min), and enzyme/protein ratio (1:3,000–1:333) were evaluated on the release of N-glycans from bovine colostrum whey by EndoBI-1. A central composite design was used, including a two-level factorial design (24) with four center points and eight axial points. In general, low pH values, longer reaction times, higher enzyme/protein ratio, and temperatures around 52°C resulted in the highest yield. The results demonstrated that bovine colostrum whey, considered to be a by/waste product, can be used as a glycan source with a yield of 20 mg N-glycan/g total protein under optimal conditions for the ranges investigated. Importantly, these processing conditions are suitable to be incorporated into routine dairy processing activities, opening the door for an entirely new class of products (released bioactive glycans and glycan-free milk). The new enzyme’s activity was also compared with a commercially available enzyme, showing that EndoBI-1 is more active on native proteins than PNGase F and can be efficiently used during pasteurization, streamlining its integration into existing processing strategies.

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Controlled Hydrolysis of Cheese Whey Proteins Using Trypsin and α-Chymotrypsin

Cited by 12 publications

References 13 publications

Producing a phenylalanine-free pool of peptides after tailored enzymatic hydrolyses of cheese whey

Producing a phenylalanine-free pool of peptides after tailored enzymatic hydrolyses of cheese whey

Hydrolysis of β-lactoglobulin by trypsin under acidic pH and analysis of the hydrolysates with MALDI–TOF–MS/MS

Characterizing the release of bioactiveN-glycans from dairy products by a novel endo-β-N-acetylglucosaminidase

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