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Pregled bibliografske jedinice broj: 590715

Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification


Lisak, Katarina; Toro-Sierra, Jose; Kulozik, Ulrich; Božanić, Rajka; Cheison, Seronei Chelulei
Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification // Journal of dairy research, 80 (2013), 1; 14-20 doi:10.1017/S0022029912000416 (međunarodna recenzija, članak, znanstveni)


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Naslov
Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification

Autori
Lisak, Katarina ; Toro-Sierra, Jose ; Kulozik, Ulrich ; Božanić, Rajka ; Cheison, Seronei Chelulei

Izvornik
Journal of dairy research (0022-0299) 80 (2013), 1; 14-20

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
α-chymotrypsin; selective whey protein hydrolysis; β-lactoglobulin; α-lactalbumin recovery; Bowman–Birk inhibitor; chicken egg-white inhibitor

Sažetak
The present study examines the resistance of the α-lactalbumin to α-chymotrypsin (EC 3.4.21.1) digestion under various experimental conditions. Whey protein isolate (WPI) was hydrolysed using randomised hydrolysis conditions (5 and 10% of WPI ; pH 7·0, 7·8 and 8·5 ; temperature 25, 37 and 50 °C ; enzyme-to-substrate ratio, E/S, of 0·1%, 0·5 and 1%). Reversed-phase high performance liquid chromatography (RP-HPLC) was used to analyse residual proteins. Heat, pH adjustment and two inhibitors (Bowman–Birk inhibitor and trypsin inhibitor from chicken egg white) were used to stop the enzyme reaction. While operating outside of the enzyme optimum it was observed that at pH 8·5 selective hydrolysis of β-lactoglobulinwas improved because of a dimer-to-monomer transition while α-la remained relatively resistant. The best conditions for the recovery of native and pure α-la were at 25 °C, pH 8·5, 1% E/S ratio, 5% WPI (w/v) while the enzyme was inhibited using Bowman–Birk inhibitor with around 81% of original α-la in WPI was recovered with no more β-lg. Operating conditions for hydrolysis away from the chymotrypsin optimum conditions offers a great potential for selective WPI hydrolysis, and removal, of β-lg with production of whey protein concentrates containing low or no β-lg and pure native α-la. This method also offers the possibility for production of β-lg-depleted milk products for sensitive populations.

Izvorni jezik
Engleski

Znanstvena područja
Prehrambena tehnologija



POVEZANOST RADA


Ustanove:
Prehrambeno-biotehnološki fakultet, Zagreb

Poveznice na cjeloviti tekst rada:

doi journals.cambridge.org dx.doi.org

Citiraj ovu publikaciju:

Lisak, Katarina; Toro-Sierra, Jose; Kulozik, Ulrich; Božanić, Rajka; Cheison, Seronei Chelulei
Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification // Journal of dairy research, 80 (2013), 1; 14-20 doi:10.1017/S0022029912000416 (međunarodna recenzija, članak, znanstveni)
Lisak, K., Toro-Sierra, J., Kulozik, U., Božanić, R. & Cheison, S. (2013) Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification. Journal of dairy research, 80 (1), 14-20 doi:10.1017/S0022029912000416.
@article{article, author = {Lisak, Katarina and Toro-Sierra, Jose and Kulozik, Ulrich and Bo\v{z}ani\'{c}, Rajka and Cheison, Seronei Chelulei}, year = {2013}, pages = {14-20}, DOI = {10.1017/S0022029912000416}, keywords = {α-chymotrypsin, selective whey protein hydrolysis, β-lactoglobulin, α-lactalbumin recovery, Bowman–Birk inhibitor, chicken egg-white inhibitor}, journal = {Journal of dairy research}, doi = {10.1017/S0022029912000416}, volume = {80}, number = {1}, issn = {0022-0299}, title = {Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification}, keyword = {α-chymotrypsin, selective whey protein hydrolysis, β-lactoglobulin, α-lactalbumin recovery, Bowman–Birk inhibitor, chicken egg-white inhibitor} }
@article{article, author = {Lisak, Katarina and Toro-Sierra, Jose and Kulozik, Ulrich and Bo\v{z}ani\'{c}, Rajka and Cheison, Seronei Chelulei}, year = {2013}, pages = {14-20}, DOI = {10.1017/S0022029912000416}, keywords = {α-chymotrypsin, selective whey protein hydrolysis, β-lactoglobulin, α-lactalbumin recovery, Bowman–Birk inhibitor, chicken egg-white inhibitor}, journal = {Journal of dairy research}, doi = {10.1017/S0022029912000416}, volume = {80}, number = {1}, issn = {0022-0299}, title = {Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification}, keyword = {α-chymotrypsin, selective whey protein hydrolysis, β-lactoglobulin, α-lactalbumin recovery, Bowman–Birk inhibitor, chicken egg-white inhibitor} }

Časopis indeksira:


  • Current Contents Connect (CCC)
  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus
  • MEDLINE


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