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of 109
pro vyhledávání: '"T. Coolbear"'
Publikováno v:
Encyclopedia of Dairy Sciences ISBN: 9780128187678
Lactic acid bacteria (LAB) generate a complex diversity of flavor compounds in dairy systems that deliver positive or negative attributes, depending on their absolute and relative levels in a product and the way in which they are released on consumpt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bde15d5e2b278ce3b040cb36e2f8ba50
https://doi.org/10.1016/b978-0-12-818766-1.00019-2
https://doi.org/10.1016/b978-0-12-818766-1.00019-2
Publikováno v:
Journal of Cereal Science. 42:185-191
A salivary proteinase from the New Zealand wheat bug ( Nysius huttoni ) was partially purified and analysed for substrate specificity by a variety of techniques on the following proteins: wheat, rye, barley and corn proteins, haemoglobin, bovine seru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::21edd2233488ef40356a515070d5294e
https://doi.org/10.1016/j.jcs.2005.04.003
https://doi.org/10.1016/j.jcs.2005.04.003
Studies on flavor generation during longer-term ripening of cheeses have revealed at least some of the diversity of flavor compounds that lactic acid bacteria (LAB) can generate in dairy systems. These compounds can deliver positive or negative attri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c1961a8cbf6f1b66b1c6fc7038150cc
https://doi.org/10.1016/b978-0-12-374407-4.00271-5
https://doi.org/10.1016/b978-0-12-374407-4.00271-5
Akademický článek
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Publikováno v:
Biochemistry and Cell Biology. 68:1292-1296
A stable DNA polymerase (EC 2.7.7.7) has been purified from the extremely thermophilic eubacterium Thermotoga sp. strain FjSS3-B.1 by a five-step purification procedure. First, the crude extract was treated with polyethylenimine to precipitate nuclei
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cb611c85e791f0e1d2410e56d6edb63
https://doi.org/10.1139/o90-192
https://doi.org/10.1139/o90-192
Publikováno v:
Gluten Proteins ISBN: 9780854046331
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::991f25053686c1dee9d9c99ab2fdafdd
https://doi.org/10.1039/9781847552099-00413
https://doi.org/10.1039/9781847552099-00413
Publikováno v:
Applied microbiology and biotechnology. 46(1)
beta-Galactosidases from Lactobacillus delbruekii subsp. bulgaricus 20056, Lb. casei 20094, Lactococcus lactis subsp. lactis 7962, Streptococcus thermophilus TS2, Pediococcus pentosaceus PE39 and Bifidobacterium bifidum 1901 were partially purified.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e748882d894374cd9310c3dfc915c11c
https://pubmed.ncbi.nlm.nih.gov/8987531
https://pubmed.ncbi.nlm.nih.gov/8987531
The enzymes from extreme thermophiles: bacterial sources, thermostabilities and industrial relevance
Publikováno v:
Advances in biochemical engineering/biotechnology. 45
This review on enzymes from extreme thermophiles (optimum growth temperature greater than 65 degrees C) concentrates on their characteristics, especially thermostabilities, and their commercial applicability. The enzymes are considered in general ter
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::b57efce07f0386ab759dd7c4a7bc554f
https://pubmed.ncbi.nlm.nih.gov/1605092
https://pubmed.ncbi.nlm.nih.gov/1605092
Publikováno v:
Applied microbiology and biotechnology. 36(3)
The action of the cell-wall-associated proteinases from Lactococcus lactis subsp. cremoris strains H2 and SK112 on bovine beta-casein was compared. The proteinase from the H2 strain was characterised as a PI-type proteinase since it did not hydrolyse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2952bf1c28f718b181cc7c0c866a1512
https://pubmed.ncbi.nlm.nih.gov/1368045
https://pubmed.ncbi.nlm.nih.gov/1368045
Publikováno v:
Meat science. 32(1)
The potential use of the thermophile enzymes E A.1 protease (from Bacillus strain E A.1), 4-1.A protease (from Thermus strain Rt4-1.A) and caldolysin (from Thermus strain T-351) in meat tenderisation has been investigated. Temperature-activity relati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f79af71e03f07a119559a00da0274ba2
https://pubmed.ncbi.nlm.nih.gov/22059725
https://pubmed.ncbi.nlm.nih.gov/22059725