EFFECT OF VARIOUS CONCENTRATIONS OF PAPAIN AND POTASSIUM lODATE ON THE LOAF VOLUME OF BREAD

نویسندگان

  • JEHIEL DAVIDSON
  • J. A. LECLERC
چکیده

The mechanism of the action of chemical bread improvers has recently been the subject of wide discussion. J0rgensen (9, 10, 11 j 12,13),^ and Balls and Hale (2, 3) have advanced the theory that the improvement of baking quality caused by oxidizing agents, such as potassium brómate and potassium iodate, is due to the fact that they inactivate the proteinases of flour, thereby inhibiting the action of these enzymes on the flour proteins. These writers also believe that the flour proteinases belong to the papain group. This theory is supported by Flohil {6) and is opposed by Read and Haas {16, 17, 18), Carbonnelle (5), and Ritter {19). The arguments for and against the theory have been fully and ably summed up by the opposing sides in recent articles {12, 13, 14 j 18). In studies on the total and free amylase content of ungerminated seeds, baking tests were made on a sample of commercial wheat flour to which were added various concentrations of papain and potassium iodate. The results, reported here, may throw some added light on the disputed theories with regard to the mechanism of action of certain bread improvers.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Effects of Ca2+ on the conformation and enzymatic activity of smooth muscle myosin.

The influence of Ca2+ on the enzymatic and physical properties of smooth muscle myosin was studied. The actin-activated ATPase activity of phosphorylated gizzard myosin and heavy meromyosin is higher in the presence of Ca2+ than in its absence, but this effect is found only at lower MgCl2 concentrations. As the MgCl2 concentration is increased, Ca2+ sensitivity is decreased. The concentration o...

متن کامل

Voltage-activated potassium channels in the plasma membrane of rod outer segments: a possible effect of enzymatic cell dissociation.

Using patch-clamp techniques, we recorded single-channel currents from the plasma membrane of the outer segment of isolated light-adapted rods. The channels are potassium-selective and their conductance is about 87 pS. The channels are activated by depolarization and are not sensitive to cytoplasmic calcium, they are exclusively found in rods isolated with the proteolytic enzyme papain, and are...

متن کامل

A Proteolytic Enzyme Produced by Group a Streptococci with Special Reference to Its Effect on the Type-specific M Antigen

1. Group A streptococci sometimes produce in broth culture an extracellular proteolytic enzyme. 2. Under suitable cultural conditions the enzyme has been demonstrated in representative cultures of most of the Griffith types. Its production by a given strain may be suppressed by serial passage through mice and the variant so produced has been found to maintain this change in character on subcult...

متن کامل

Attempted isolation of a heparin proteoglycan from bovine liver capsule.

(1) Polysaccharides were isolated from bovine liver capsule by extraction with 2m-potassium chloride followed by precipitation from 0.8m-potassium chloride with cetylpyridinium chloride. Chondroitin sulphate was eliminated by digestion with hyaluronidase. The yield of heparin was approx. 40% of that obtained after extraction of the papain-digested tissue. (2) The macromolecular properties of th...

متن کامل

Immunological and chemical purity of papain-solubilized HL-A antigens.

Three preparations of purified papain-solublized HL-A antigens have been radiolabeled by reductive methylation using formaldehyde and potassium boro[3H]hydride, and their reaction with specific HL-A antisera has been investigated. Greater than 99 percent of the radioactivity in the [3H]HL-A2 preparation could be complexed with several HL-A2 antisera, but not with specificity controls. The other...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2010