Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
Collection
Years
  • 1
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Two electrophoretically homogeneous proteinases designated proteinase A and B were isolated from anchovy viscera. Purity was increased 17.7 and 24.6-fold with approximately 1.9 and 1.8% yield for proteinases A and B, respectively. The maximum caseinolytic activity was found to be at pH 9.4 for proteinase A and at pH 9.6 for proteinase B at the optimum temperature of 48°C. The molecular weights of proteinase A and B were determined to be 27, 300 and 25,100 D, respectively, using Sephadex G-100 gel filtration. The amino acid profiles of the enzymes were similar and relative proportion of amino acid residues was comparable to that in bovine pancreatic α-chymotrypsin. Proteinase A and B were identified as α-chymottypsin-like serine proteases by inhibitor and substrate specificity studies. Apparent Km (Km′) values of proteinase A and B for benzoyl-L-tyrosine ethyl ester were 4.6 × 10−4 M and 1.2 × 10−3 M, respectively.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 2
    ISSN: 1745-4514
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Proteases recovered from Northern pink shrimp (NPS) and Southern rough shrimp (SS) processing discards (heads, shells, tails) were characterized. Shrimp processing discards were extracted with water following homogenization and centrifugation in order to obtain the crude extract which was subsequently fractionated with solid ammonium sulfate. Two fractions sedimenting with 30–50% (designated as NPS-I and SS-I), and 50–70% (designated as NPS-II and SS-II) ammonium sulfate were collected following centrifugation, respectively. Endoprotease activity of the crude extract was 0.02 U/mg for hemoglobin (Hb, pH 3.0), 0.16 U/mg for azocasein (Ac, pH 6.0) and 0.12 U/mg for benzoyl-Arg-β-naphthylamide (BANA, pH 7.0). The exoprotease activity was 0.11–0.17 U/mg for Arg-β-naphthylamide (ArgNA, pH 7.0), 0.06–0.11 U/mg for Lys-β-naphthylamide (LysNA, pH 7.0) and 0.08–0.09 U/mg for Leu-β-naphthylamide (LeuNA, pH 7.0). Endoprotease activity increased 5–7.4 fold for NPS-I and SS-I, and 1.9–2.7 fold for NPS-II and SS-II against crude extract. Meanwhile, exoprotease activity increased 3.6–4.8 fold for NPS-I and SS-I, and 5.6–7.2 fold for NPS-II and SS-II. Meat treated with NPS-I and SS-I was tenderized more extensively than that treated with NPS-II and SS-II. The results of this study suggest that proteases recovered from shrimp processing discards may potentially be used as processing aids in formulated foods.
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
  • 3
    ISSN: 1745-4522
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The antioxidant activity of an extract of a marine red alga (Grateloupia filicina) was evaluated in linoleic acid and fish oil induct period oil at 65C. Oxidative stability of the oils was evaluated by employing peroxide value (PV), 2-thiobarbituric acid reactive substances (TBARS), conjugated diene (CD) and weight gain experiments. The algal extract was applied to linoleic acid and fish oil at 0.01, 0.03 and 0.05% and results were compared with those of commercial antioxidants such as butylated hydroxytoluene (BHT), butylated hydroxyanisol (BHA) and α-tocopherol at 0.01 %. Results indicated the ability of the alga extract to inhibit oxidation of linoleic acid and fish oil; at α 0.05%
    Type of Medium: Electronic Resource
    Signatur Availability
    BibTip Others were also interested in ...
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...