The action of chymosin on κ-casein and its macropeptide: Effect of pH and analysis of products of secondary hydrolysis

Reid, Julian R.; Coolbear, Tim; Ayers, John S.; Coolbear, K. P.

doi:10.1016/s0958-6946(97)00062-9

Cited by 38 publications

(22 citation statements)

References 25 publications

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“…3 b Co-elution at day 1. Area of single peak increases with decreasing salt content (↑) c A systematic increase and decrease in peak area (A210 nm) as a function of decreasing salt content is denoted by ↑ and ↓, respectively d Peak area of low-salt cheese was larger than the rest, which all had similar areas e Peak area of high-salt cheese was smaller than the rest, which all had similar areas f Previous studies reporting cleavage sites of PLA, CEP, CHY and PepO g Sousa et al 2001 h Exterkate and Alting (1995) i Exterkate et al (1997) j Møller et al (unpublished) k Reid and Coolbear (1999) l Guillou et al (1991) m Baankreis et al (1995) n McSweeney et al (1994) o Reid et al (1997) p Larsson et al (2006) CEP activity towards α S1 -CN 16/17 cleavage. It follows from the effect of salt on early α S1 -CN(f1-9/13) accumulation that more α S1 -CN(f1-23) substrate was available for α S1 -CN(f1-16) formation at decreasing salt concentration.…”

Section: Peptide Formation and Degradationmentioning

confidence: 91%

Manufacture and biochemical characteristics during ripening of Cheddar cheese with variable NaCl and equal moisture content

Møller

Rattray

Høier

et al. 2012

Dairy Sci. & Technol.

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Reduction of salt in ripened cheese presents an industry challenge due to its profound role in flavour and texture development. This study investigated the biochemical impact of varying the salt concentration in Cheddar cheese while maintaining the moisture content constant, with particular emphasis on proteolysis. Cheeses containing 0.9, 1.3, 1.8 and 2.4 % (w/w) salt and 37.7±0.2 % (w/w) moisture were manufactured by parallel adjustment of the curd grain size, cooking temperature and time, cheddaring, curd chip size and rate of salting and analysed over the course of 270 days ripening. Salt reduction affected chymosin and starter lactocepin activities to accelerate casein degradation and accumulate derived peptides at rates correlating positively or (mostly) inversely with salt concentration. The kinetics of α S1 -CN (f1-23) and N-terminal peptides produced thereof and of β-CN(f193-209) were studied in detail. Plasmin activity was affected by cooking treatment and (small) pH differences during ripening but appeared limited overall, due to low levels of pH. Starter lysis showed a strong positive dependency on the salt concentration, and resultant lower contents of free amino acids upon salt reduction were evident. In essence, salt reduction caused a marked decrease in the ratio of peptidase to proteinase activity. Remedies to counterbalance this ratio were discussed in order to avoid excessive accumulation of bitter peptides and promote the stage of maturity. Salt

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Section: Peptide Formation and Degradationmentioning

confidence: 91%

Manufacture and biochemical characteristics during ripening of Cheddar cheese with variable NaCl and equal moisture content

Møller

Rattray

Høier

et al. 2012

Dairy Sci. & Technol.

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“…Most of the analytical methods for CMP determination were focused on the identification of rennet whey solids in adulterated skim milk or buttermilk powder (Olieman & van Riel, 1989;Ferreira & Oliveira, 2003) as well as to study the release of CMP during the renneting process (Calvo, 2002;Coolbear, Elgar, Coolbear, & Ayers, 1996;Reid, Coolbear, Ayers, & Coolbear, 1997;Sharma, Hill, & Mittal, 1993). These methods analysed the non-glycosylated CMP of variant A (CMP A) as a single peak or the CMP group as multiple unresolved peaks.…”

Section: Introductionmentioning

confidence: 99%

Precipitation behaviour of caseinomacropeptides and their simultaneous determination with whey proteins by RP-HPLC

Thomä

Krause²,

Kulozik

2006

International Dairy Journal

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“…A number of peptides were identified in the samples. These matches peptides reported to originate from bovine derived proteases, such as plasmin, cathesin D and elastase (Considine et al, 2004;Hurley et al, 2000;Le Bars and Gripon, 1993), as well as bacterial proteases from Lactobacillus helveticus and thermolysin (Robert et al, 2004), or industrially applied proteases such as chymosin (Reid et al, 1997). Further studies will be made to profile these peptide fractions -and hopefully identify a link between the presence and/or quantity of specific peptides, proteases and the quality of the products.…”

Section: Introductionmentioning

confidence: 66%

Peptidomics in extended shelf life dairy products, for assessment of proteolysis and product quality

Villumsen

Hammershøj

Larsen

et al. 2013

Farm Animal Proteomics 2013

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Important notes:Do NOT write outside the grey boxes. Any text or images outside the boxes will be deleted. Do NOT alter the structure of this form. Simply enter your information into the boxes. The form will be automatically processed -if you alter its structure your submission will not be processed correctly.Do not include keywords -you can add them when you submit the abstract online. Title Abstract:Whey is used as an ingredient in long shelf life sports drinks due to its high nutritional value. However, some liquid Whey Protein Isolate (WPI) based products develop insoluble material during shelf time; a phenomenon referred to as "unwanted protein aggregation". In many cases this deterioration can be avoided, by increasing the heat treatments from 95⁰C/180s to 120⁰C/20s. A fluorescence amine assay that monitors the level of free amino terminals (Larsen et al., 2004) has shown that the products subjected to the mild heat treatment have an increase in amino terminals during storage which is more than twice as high as the increase observed in the more harsh heat treated products. This indicates a presence of proteolytic activity from heat stable proteases in products having undergone both types of heat treatments, but also a heat treatment dependent inactivation of the respective proteases. Therefore a mass spectrometry (MS) based peptidomic approach was initiated to characterize the peptide fraction of the WPIs, with the aim of identifying a relation between the peptide profiles and the product quality of the re-dissolved WPIs during storage and furthermore to deduce information about the proteolytic activity and the identity of the proteases. Redissolved WPIs were adjusted to pH 3 to simulate the sports drinks conditions and subsequently subjected to heat treatments. After two weeks of storage at room temperature the peptide fractions of the samples were isolated using centrifugal filter units with a cutoff of 10kDa and 3kDa and the permeates were desalted and concentrated on handmade chromatographic columns as described by Gobom et al, (1999). By means of MALDI-TOF-TOF, this peptide fraction was subjected to MS/MS and mass searches were carried out using the SwissProt database.

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The action of chymosin on κ-casein and its macropeptide: Effect of pH and analysis of products of secondary hydrolysis

Cited by 38 publications

References 25 publications

Manufacture and biochemical characteristics during ripening of Cheddar cheese with variable NaCl and equal moisture content

Manufacture and biochemical characteristics during ripening of Cheddar cheese with variable NaCl and equal moisture content

Precipitation behaviour of caseinomacropeptides and their simultaneous determination with whey proteins by RP-HPLC

Peptidomics in extended shelf life dairy products, for assessment of proteolysis and product quality

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