Advanced Search
Display options
Filter resources
Text Availability
Article type
Publication date
Species
Language
Sex
Age
Showing 13 to 24 of 361 entries
Sorted by: Best Match Show Resources per page
The salting-out of amino-acids from protein hydrolysates: The isolation of tyrosine, leucine and methionine.

The Biochemical journal

Hill EM, Robson W.
PMID: 16745446
Biochem J. 1934;28(3):1008-13. doi: 10.1042/bj0281008.

No abstract available.

Cite
Hill EM, Robson W. The salting-out of amino-acids from protein hydrolysates: The isolation of tyrosine, leucine and methionine. Biochem J. 1934;28(3):1008-13doi: 10.1042/bj0281008.
Hill, E. M., & Robson, W. (1934). The salting-out of amino-acids from protein hydrolysates: The isolation of tyrosine, leucine and methionine. The Biochemical journal, 28(3), 1008-13. https://doi.org/10.1042/bj0281008
Hill, E M, and Robson, W. "The salting-out of amino-acids from protein hydrolysates: The isolation of tyrosine, leucine and methionine." The Biochemical journal vol. 28,3 (1934): 1008-13. doi: https://doi.org/10.1042/bj0281008
Hill EM, Robson W. The salting-out of amino-acids from protein hydrolysates: The isolation of tyrosine, leucine and methionine. Biochem J. 1934;28(3):1008-13. doi: 10.1042/bj0281008. PMID: 16745446; PMCID: PMC1253294.
Copy Download .nbib Format: NLM
The micro-determination of glycine in protein hydrolysates.

The Biochemical journal

Town BW.
PMID: 16746229
Biochem J. 1936 Oct;30(10):1833-6. doi: 10.1042/bj0301833.

No abstract available.

Cite
Town BW. The micro-determination of glycine in protein hydrolysates. Biochem J. 1936;30(10):1833-6doi: 10.1042/bj0301833.
Town, B. W. (1936). The micro-determination of glycine in protein hydrolysates. The Biochemical journal, 30(10), 1833-6. https://doi.org/10.1042/bj0301833
Town, B W. "The micro-determination of glycine in protein hydrolysates." The Biochemical journal vol. 30,10 (1936): 1833-6. doi: https://doi.org/10.1042/bj0301833
Town BW. The micro-determination of glycine in protein hydrolysates. Biochem J. 1936 Oct;30(10):1833-6. doi: 10.1042/bj0301833. PMID: 16746229; PMCID: PMC1263267.
Copy Download .nbib Format: NLM
Critique of the Foreman method for the estimation of the dicarboxylic acids in protein hydrolysates.

The Biochemical journal

Bailey K, Chibnall AC, Rees MW, Williams EF.
PMID: 16747653
Biochem J. 1943 Sep;37(3):360-72. doi: 10.1042/bj0370360.

No abstract available.

Cite
Bailey K, Chibnall AC, Rees MW, et al. Critique of the Foreman method for the estimation of the dicarboxylic acids in protein hydrolysates. Biochem J. 1943;37(3):360-72doi: 10.1042/bj0370360.
Bailey, K., Chibnall, A. C., Rees, M. W., & Williams, E. F. (1943). Critique of the Foreman method for the estimation of the dicarboxylic acids in protein hydrolysates. The Biochemical journal, 37(3), 360-72. https://doi.org/10.1042/bj0370360
Bailey, K, et al. "Critique of the Foreman method for the estimation of the dicarboxylic acids in protein hydrolysates." The Biochemical journal vol. 37,3 (1943): 360-72. doi: https://doi.org/10.1042/bj0370360
Bailey K, Chibnall AC, Rees MW, Williams EF. Critique of the Foreman method for the estimation of the dicarboxylic acids in protein hydrolysates. Biochem J. 1943 Sep;37(3):360-72. doi: 10.1042/bj0370360. PMID: 16747653; PMCID: PMC1257918.
Copy Download .nbib Format: NLM
Protein hydrolysates in sports nutrition.

Nutrition & metabolism

Manninen AH.
PMID: 19785737
Nutr Metab (Lond). 2009 Sep 28;6:38. doi: 10.1186/1743-7075-6-38.

It has been suggested that protein hydrolysates providing mainly di- and tripeptides are superior to intact (whole) proteins and free amino acids in terms of skeletal muscle protein anabolism. This review provides a critical examination of protein hydrolysate studies...

Cite
Manninen AH. Protein hydrolysates in sports nutrition. Nutr Metab (Lond). 2009;6:38doi: 10.1186/1743-7075-6-38.
Manninen, A. H. (2009). Protein hydrolysates in sports nutrition. Nutrition & metabolism, 638. https://doi.org/10.1186/1743-7075-6-38
Manninen, Anssi H. "Protein hydrolysates in sports nutrition." Nutrition & metabolism vol. 6 (2009): 38. doi: https://doi.org/10.1186/1743-7075-6-38
Manninen AH. Protein hydrolysates in sports nutrition. Nutr Metab (Lond). 2009 Sep 28;6:38. doi: 10.1186/1743-7075-6-38. PMID: 19785737; PMCID: PMC2761917.
Copy Download .nbib Format: NLM
Formation of stable bdelloplasts as a starvation-survival strategy of marine bdellovibrios.

Applied and environmental microbiology

Sánchez-Amat A, Torrella F.
PMID: 16348280
Appl Environ Microbiol. 1990 Sep;56(9):2717-25. doi: 10.1128/aem.56.9.2717-2725.1990.

Several wild-type isolates of marine bdellovibrios formed stable bdelloplasts when they infected gram-negative bacterial prey under certain culture conditions. Synchronous predator-prey cultures and low nutrient concentrations increased the yield of stable bdelloplasts. The bdellovibrio cells retained in the stable...

Cite
Sánchez-Amat A, Torrella F. Formation of stable bdelloplasts as a starvation-survival strategy of marine bdellovibrios. Appl Environ Microbiol. 1990;56(9):2717-25doi: 10.1128/aem.56.9.2717-2725.1990.
Sánchez-Amat, A., & Torrella, F. (1990). Formation of stable bdelloplasts as a starvation-survival strategy of marine bdellovibrios. Applied and environmental microbiology, 56(9), 2717-25. https://doi.org/10.1128/aem.56.9.2717-2725.1990
Sánchez-Amat, A, and Torrella, F. "Formation of stable bdelloplasts as a starvation-survival strategy of marine bdellovibrios." Applied and environmental microbiology vol. 56,9 (1990): 2717-25. doi: https://doi.org/10.1128/aem.56.9.2717-2725.1990
Sánchez-Amat A, Torrella F. Formation of stable bdelloplasts as a starvation-survival strategy of marine bdellovibrios. Appl Environ Microbiol. 1990 Sep;56(9):2717-25. doi: 10.1128/aem.56.9.2717-2725.1990. PMID: 16348280; PMCID: PMC184833.
Copy Download .nbib Format: NLM
Protein hydrolysates from meat industry by-products.

Meat science

Webster JD, Ledward DA, Lawrie RA.
PMID: 22055137
Meat Sci. 1982 Sep;7(2):147-57. doi: 10.1016/0309-1740(82)90080-8.

Hydrolysates were prepared from bovine lung, bovine rumen and from partially defatted tissue by treatment at 50°C with either pepsin at pH 3·0, papain at pH 5·5, neutrase at pH 7·0 or alcalase at pH 8·5. For all substrates...

Cite
Webster JD, Ledward DA, Lawrie RA. Protein hydrolysates from meat industry by-products. Meat Sci. 1982;7(2):147-57doi: 10.1016/0309-1740(82)90080-8.
Webster, J. D., Ledward, D. A., & Lawrie, R. A. (1982). Protein hydrolysates from meat industry by-products. Meat science, 7(2), 147-57. https://doi.org/10.1016/0309-1740(82)90080-8
Webster, J D, et al. "Protein hydrolysates from meat industry by-products." Meat science vol. 7,2 (1982): 147-57. doi: https://doi.org/10.1016/0309-1740(82)90080-8
Webster JD, Ledward DA, Lawrie RA. Protein hydrolysates from meat industry by-products. Meat Sci. 1982 Sep;7(2):147-57. doi: 10.1016/0309-1740(82)90080-8. PMID: 22055137.
Copy Download .nbib Format: NLM
Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology.

Journal of food science and technology

Dey SS, Dora KC.
PMID: 24426043
J Food Sci Technol. 2014 Jan;51(1):16-24. doi: 10.1007/s13197-011-0455-4. Epub 2011 Jul 23.

Protein hydrolysates were produced from shrimp waste mainly comprising head and shell of Penaeus monodon by enzymatic hydrolysis for 90 min using four microbial proteases (Alcalase, Neutrase, Protamex, Flavourzyme) where PR(%) and DH (%) of respective enzymes were compared...

Cite
Dey SS, Dora KC. Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology. J Food Sci Technol. 2011;51(1):16-24doi: 10.1007/s13197-011-0455-4.
Dey, S. S., & Dora, K. C. (2014). Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology. Journal of food science and technology, 51(1), 16-24. https://doi.org/10.1007/s13197-011-0455-4
Dey, Satya S, and Dora, Krushna Chandra. "Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology." Journal of food science and technology vol. 51,1 (2014): 16-24. doi: https://doi.org/10.1007/s13197-011-0455-4
Dey SS, Dora KC. Optimization of the production of shrimp waste protein hydrolysate using microbial proteases adopting response surface methodology. J Food Sci Technol. 2014 Jan;51(1):16-24. doi: 10.1007/s13197-011-0455-4. Epub 2011 Jul 23. PMID: 24426043; PMCID: PMC3857399.
Copy Download .nbib Format: NLM
Production, active staining and gas chromatography assay analysis of recombinant aminopeptidase P from Lactococcus lactis ssp. lactis DSM 20481.

AMB Express

Stressler T, Eisele T, Schlayer M, Fischer L.
PMID: 22853547
AMB Express. 2012 Aug 01;2(1):39. doi: 10.1186/2191-0855-2-39.

The aminopeptidase P (PepP, EC 3.4.11.9) gene from Lactococcus lactis ssp. lactis DSM 20481 was cloned, sequenced and expressed recombinantly in E. coli BL21 (DE3) for the first time. PepP is involved in the hydrolysis of proline-rich proteins and,...

Cite
Stressler T, Eisele T, Schlayer M, et al. Production, active staining and gas chromatography assay analysis of recombinant aminopeptidase P from Lactococcus lactis ssp. lactis DSM 20481. AMB Express. 2012;2(1):39doi: 10.1186/2191-0855-2-39.
Stressler, T., Eisele, T., Schlayer, M., & Fischer, L. (2012). Production, active staining and gas chromatography assay analysis of recombinant aminopeptidase P from Lactococcus lactis ssp. lactis DSM 20481. AMB Express, 2(1), 39. https://doi.org/10.1186/2191-0855-2-39
Stressler, Timo, et al. "Production, active staining and gas chromatography assay analysis of recombinant aminopeptidase P from Lactococcus lactis ssp. lactis DSM 20481." AMB Express vol. 2,1 (2012): 39. doi: https://doi.org/10.1186/2191-0855-2-39
Stressler T, Eisele T, Schlayer M, Fischer L. Production, active staining and gas chromatography assay analysis of recombinant aminopeptidase P from Lactococcus lactis ssp. lactis DSM 20481. AMB Express. 2012 Aug 01;2(1):39. doi: 10.1186/2191-0855-2-39. PMID: 22853547; PMCID: PMC3418211.
Copy Download .nbib Format: NLM
Synthesis and in vitro antioxidant functions of protein hydrolysate from backbones of Rastrelliger kanagurta by proteolytic enzymes.

Saudi journal of biological sciences

Sheriff SA, Sundaram B, Ramamoorthy B, Ponnusamy P.
PMID: 24596496
Saudi J Biol Sci. 2014 Jan;21(1):19-26. doi: 10.1016/j.sjbs.2013.04.009. Epub 2013 May 06.

Every year, a huge quantity of fishery wastes and by-products are generated by fish processing industries. These wastes are either underutilized to produce low market value products or dumped leading to environmental issues. Complete utilization of fishery wastes for...

Cite
Sheriff SA, Sundaram B, Ramamoorthy B, et al. Synthesis and in vitro antioxidant functions of protein hydrolysate from backbones of Rastrelliger kanagurta by proteolytic enzymes. Saudi J Biol Sci. 2013;21(1):19-26doi: 10.1016/j.sjbs.2013.04.009.
Sheriff, S. A., Sundaram, B., Ramamoorthy, B., & Ponnusamy, P. (2014). Synthesis and in vitro antioxidant functions of protein hydrolysate from backbones of Rastrelliger kanagurta by proteolytic enzymes. Saudi journal of biological sciences, 21(1), 19-26. https://doi.org/10.1016/j.sjbs.2013.04.009
Sheriff, Sheik Abdulazeez, et al. "Synthesis and in vitro antioxidant functions of protein hydrolysate from backbones of Rastrelliger kanagurta by proteolytic enzymes." Saudi journal of biological sciences vol. 21,1 (2014): 19-26. doi: https://doi.org/10.1016/j.sjbs.2013.04.009
Sheriff SA, Sundaram B, Ramamoorthy B, Ponnusamy P. Synthesis and in vitro antioxidant functions of protein hydrolysate from backbones of Rastrelliger kanagurta by proteolytic enzymes. Saudi J Biol Sci. 2014 Jan;21(1):19-26. doi: 10.1016/j.sjbs.2013.04.009. Epub 2013 May 06. PMID: 24596496; PMCID: PMC3937463.
Copy Download .nbib Format: NLM
Purification and characterisation of a new antioxidant peptide from chickpea (Cicer arietium L.) protein hydrolysates.

Food chemistry

Zhang T, Li Y, Miao M, Jiang B.
PMID: 25214325
Food Chem. 2011 Sep 01;128(1):28-33. doi: 10.1016/j.foodchem.2011.02.072. Epub 2011 Feb 24.

An antioxidant peptide was purified using consecutive chromatographic methods from chickpea protein hydrolysates (CPH). This peptide was designated as Fra.7. It had a molecular weight of 717.37Da, and its amino acid sequence was identified as Asn-Arg-Tyr-His-Glu by an ABI...

Cite
Zhang T, Li Y, Miao M, et al. Purification and characterisation of a new antioxidant peptide from chickpea (Cicer arietium L.) protein hydrolysates. Food Chem. 2011;128(1):28-33doi: 10.1016/j.foodchem.2011.02.072.
Zhang, T., Li, Y., Miao, M., & Jiang, B. (2011). Purification and characterisation of a new antioxidant peptide from chickpea (Cicer arietium L.) protein hydrolysates. Food chemistry, 128(1), 28-33. https://doi.org/10.1016/j.foodchem.2011.02.072
Zhang, Tao, et al. "Purification and characterisation of a new antioxidant peptide from chickpea (Cicer arietium L.) protein hydrolysates." Food chemistry vol. 128,1 (2011): 28-33. doi: https://doi.org/10.1016/j.foodchem.2011.02.072
Zhang T, Li Y, Miao M, Jiang B. Purification and characterisation of a new antioxidant peptide from chickpea (Cicer arietium L.) protein hydrolysates. Food Chem. 2011 Sep 01;128(1):28-33. doi: 10.1016/j.foodchem.2011.02.072. Epub 2011 Feb 24. PMID: 25214325.
Copy Download .nbib Format: NLM
Efficacy of a fish protein hydrolysate in malnourished children.

Indian journal of clinical biochemistry : IJCB

Nesse KO, Nagalakshmi AP, Marimuthu P, Singh M.
PMID: 23024471
Indian J Clin Biochem. 2011 Oct;26(4):360-5. doi: 10.1007/s12291-011-0145-z. Epub 2011 Jul 15.

UNLABELLED: Protein hydrolysates are good nutritional supplements as their bioactive ingredients can be easily absorbed and utilized for various metabolic activities. A fish protein hydrolysate (Amizate), prepared by a unique process of hydrolysis has the advantage of high di/tri...

Cite
Nesse KO, Nagalakshmi AP, Marimuthu P, et al. Efficacy of a fish protein hydrolysate in malnourished children. Indian J Clin Biochem. 2011;26(4):360-5doi: 10.1007/s12291-011-0145-z.
Nesse, K. O., Nagalakshmi, A. P., Marimuthu, P., & Singh, M. (2011). Efficacy of a fish protein hydrolysate in malnourished children. Indian journal of clinical biochemistry : IJCB, 26(4), 360-5. https://doi.org/10.1007/s12291-011-0145-z
Nesse, Knut Olav, et al. "Efficacy of a fish protein hydrolysate in malnourished children." Indian journal of clinical biochemistry : IJCB vol. 26,4 (2011): 360-5. doi: https://doi.org/10.1007/s12291-011-0145-z
Nesse KO, Nagalakshmi AP, Marimuthu P, Singh M. Efficacy of a fish protein hydrolysate in malnourished children. Indian J Clin Biochem. 2011 Oct;26(4):360-5. doi: 10.1007/s12291-011-0145-z. Epub 2011 Jul 15. PMID: 23024471; PMCID: PMC3210250.
Copy Download .nbib Format: NLM
Enhancement of the Stability and Anti-DPPIV Activity of Hempseed Hydrolysates Through Self-Assembling Peptide-Based Hydrogels.

Frontiers in chemistry

Lammi C, Bollati C, Gelain F, Arnoldi A, Pugliese R.
PMID: 30733941
Front Chem. 2019 Jan 24;6:670. doi: 10.3389/fchem.2018.00670. eCollection 2018.

Although there is an increasing interest for bioactive food protein hydrolysates as valuable ingredients for functional food and dietary supplement formulations, their potential applications are hampered by their insufficient stability in physiological conditions. In this study, an innovative strategy...

Cite
Lammi C, Bollati C, Gelain F, et al. Enhancement of the Stability and Anti-DPPIV Activity of Hempseed Hydrolysates Through Self-Assembling Peptide-Based Hydrogels. Front Chem. 2019;6:670doi: 10.3389/fchem.2018.00670.
Lammi, C., Bollati, C., Gelain, F., Arnoldi, A., & Pugliese, R. (2018). Enhancement of the Stability and Anti-DPPIV Activity of Hempseed Hydrolysates Through Self-Assembling Peptide-Based Hydrogels. Frontiers in chemistry, 6670. https://doi.org/10.3389/fchem.2018.00670
Lammi, Carmen, et al. "Enhancement of the Stability and Anti-DPPIV Activity of Hempseed Hydrolysates Through Self-Assembling Peptide-Based Hydrogels." Frontiers in chemistry vol. 6 (2018): 670. doi: https://doi.org/10.3389/fchem.2018.00670
Lammi C, Bollati C, Gelain F, Arnoldi A, Pugliese R. Enhancement of the Stability and Anti-DPPIV Activity of Hempseed Hydrolysates Through Self-Assembling Peptide-Based Hydrogels. Front Chem. 2019 Jan 24;6:670. doi: 10.3389/fchem.2018.00670. eCollection 2018. PMID: 30733941; PMCID: PMC6353790.
Copy Download .nbib Format: NLM
Showing 13 to 24 of 361 entries