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Storage and lyophilization effects of extracts of Cynara cardunculus on the degradation of ovine and caprine caseins
Open accessAbstract
Clotting and proteolytic activities are important parameters when evaluating rennets for cheesemaking. Both these activities were determined for extracts of the plant Cynara cardunculus in fresh form and after lyophilization followed by reconstitution, either in water or in citrate buffer (pH 5.4) and stored for up to 4 weeks at 4 degrees C. The patterns of degradation of ovine and caprine caseins were followed by urea polyacrylamide gel electrophoresis in attempts to qualitatively differentiate the activity of the enzyme extracts as storage time elapsed. Storage at 4 degrees C significantly decreased the clotting power of the extracts but lyophilization retarded this decrease; beta- and alpha(s)-casein breakdown generally increased with storage time, via patterns that depend on caseinate type and extract used, but lyophilized extracts reconstituted in citrate buffer were significantly less proteolytic than the other extracts. Therefore, it is suggested that lyophilized extracts (reconstituted with citrate buffer) of flowers of C. cardunculus be used rather than fresh extracts.
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“The rates of breakdown of β-and α scaseins by extracts of C. cardunculus were not significantly affected by storage time; however, lyophilised extracts reconstituted in citrate buffer were significantly less proteolytic [60].”
From Advances in the role of a plant coagulant ( Cynara cardunculus ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [60]
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“however, lyophilised extracts reconstituted in citrate buffer were significantly less proteolytic [60].”
From Advances in the role of a plant coagulant ( Cynara cardunculus ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [60]
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“The lyophilisation process seemed to retard loss of the clotting activity throughout storage, and to prevent proteolytic breakdown of the milk caseins when the extracts were reconstituted in citrate.”
From Advances in the role of a plant coagulant ( Cynara cardunculus ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [60]
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“Tavaria et al. [60] reported that storage at 4 ºC decreased significantly the clotting activity of the extracts to a greater extent in fresh than in lyophilised form.”
From Advances in the role of a plant coagulant ( Cynara cardunculus ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [60]
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In the citing paper
“The lyophilisation process seemed to retard loss of the clotting activity throughout storage, and to prevent proteolytic breakdown of the milk caseins when the extracts were reconstituted in citrate.”
From Advances in the role of a plant coagulant ( Cynara cardunculus ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [60]
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“This is in agreement with Tavaria et al. [60], who reported that ovine β-casein is degraded by 48.2%, whereas caprine β-casein is degraded by 68.9%, both in caseinate form.”
From Advances in the role of a plant coagulant ( Cynara cardunculus ) in vitro and during ripening of cheeses from several milk species (2002) · cites this paper as [60]
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Citations
Cites
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Flagged first, then by citations
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Cited by
Sorted by citations
Chazarra, S., Sidrach, L., López-Molina, D., & Rodríguez-López, J. N. (2007) · International Dairy Journal · doi:10.1016/j.idairyj.2007.04.010 · Cited by 110
Sousa, M. J., & Malcata, F. X. (2002) · Le Lait · doi:10.1051/lait:2002001 · Cited by 84
Self-citationReligiosin B, a milk-clotting serine protease from Ficus religiosa
Kumari, M., Sharma, A., & Jagannadham, M. V. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2011.09.122 · Cited by 69
Metadata
- Authors
- Tavaria, F. K., Sousa, M. J., & Malcata, F. X.
- Affiliations
- Universidade Católica Portuguesa (PT)
- Corresponding author
- Malcata, F.Xavier
- Venue
- Food Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 72
- Issue
- 1
- Pages
- 79-88
- ISSN
- 0308-8146 (ISSN-L)
- OpenAlex
- W1982604066
- Cited by
- 32
- References
- 1
- Citations by year
- 2023: 1 · 2022: 1 · 2020: 1 · 2019: 4 · 2018: 1 · 2017: 3 · 2016: 3 · 2015: 2 · 2014: 4 · 2013: 1 · 2012: 2
- FWCI
- 0.43
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Food Chemistry (publishedVersion)
- Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, other-oa)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Cynara cardunculus studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Keywords
- Cynara cardunculus, artichoke, freeze-drying, storage stability, casein degradation, β-casein, alpha-casein, proteolytic activity
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