Soybean phosphatase. Purification and properties

Mayer, Frank; Campbell, Rebecca A.; Smith, A. K.; McKinney, L. L.

doi:10.1016/0003-9861(61)90044-3

Cited by 26 publications

(5 citation statements)

References 9 publications

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“…The optimum for the disappearance of phytate in bean at 50°C lies in the range of pH 5.0-5.5. Various (Mayer et al 1961), 5.2 for dwarf French beans (Phaseolus vulgaris) (Gibbins and Norris 1963), 7.5 for mung beans (Mandal 1972), and 5.3 for Sanilac navy beans (Lolas and Markakis 1976). Since most plant phytases are almost completely destroyed below pH 2.5, it is unlikely that phytase from dietary sources would survive the acidic conditions of the stomach.…”

Section: Effect Of Phmentioning

confidence: 99%

“…In the latter case, however, it stops at approximately 50% conversion. Although phytase activity, reviewed by Sloane-Stanley (1961), has been demonstrated and the enzyme(s) have been purified and characterized in soybeans (Mayer et al 1961), in various germinating seeds (Chang 1967;Mayer 1958;Gibbins and Norris 1963), including germinating mung beans (Mandal et al 1972), no formal, direct demonstration of its presence in dry ungerminated beans has appeared in the literature until quite recently (Chang 1975;Lolas and Markakis 1976). In the present investigation we demonstrate the presence of phytase, albeit feeble and elusive, in extracts of dry common beans and present a procedure for its concentration and partial enrichment.…”

Section: Introductionmentioning

confidence: 99%

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Characterization of Phytase of Beans (Phaseolus Vulgaris)

Chang

Schwimmer

1977

J Food Biochemistry

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Phytase from California Small White beans was extracted, concentrated and enriched by heat treatment and ammonium sulfate fractionation. Crude enzyme fractions tenaciously retained endogenous phytate which could be removed by autolysis at 45°C and p H 5.2. Characterization o f the phytase preparation showed: (1) increase in activity with increasing temperature from 37 to 60°C, ( 2 ) an activation energy of approximately 9,200 cal/mole f o r the hydrolysis of inositol hexaphosphate; ( 3 ) p H optimum o f 5.2; (4) a Km value of 2.22 X 1C4M;( 5 ) apparently partial inhibition at high substrate concentrations; ( 6 ) fully competitive inhibition by one o f the reaction products, inorganic phosphate, with Ki = 3.1 X 104M. These properties and kinetic constants are comparable to those reported f o r phytase preparations from similar sources and they adequately account for in situ autolytic loss of phytic acid from these beans.

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Section: Effect Of Phmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization of Phytase of Beans (Phaseolus Vulgaris)

Chang

Schwimmer

1977

J Food Biochemistry

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“…Selective enzymatic hydrolysis of phytate phosphorus should release the phosphorus in a form available to the animal. Enzymes of this type have been found in wheat bran (9), in various plant seeds (7,8,11), in plant storage organs such as potato (6), in tobacco leaves (13), and have been obtained from microorganisms (1,3,5,12). This paper describes the screening of various microorganisms to determine which ones are producers of highly active extracellular acid phytase.…”

mentioning

confidence: 99%

Survey of Microorganisms for the Production of Extracellular Phytase

Shieh¹,

Ware²

1968

Applied Microbiology

128

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A culture enrichment technique was used to isolate phytase-producing microorganisms. Also, microorganisms from various culture collections were tested for their phytase-producing ability. A number of the Aspergillus niger group produced extracellular phytase which dephosphorylated calcium phytate in acidic solution. A soil isolate, A. ficuum NRRL 3135, produced the most active phytase in a cornstarch-based medium. Production of phytase was strongly repressed by inorganic phosphates and required a high carbon to phosphorus ratio in the medium.

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“…Phosphorylase activity of the tissue extracts was determined by measuring the phosphate produced from the glucose-1-phosphate dependent synthesis of starch by phosphorylase (Whelan 1955) except that the reaction mixture contained 0.025 M NaF to inhibit phosphatases (Mayer £/ al. 1961).…”

Section: Phosphorylase Assaymentioning

confidence: 99%

Role of β‐amylase in starch metabolism during soybean seed development and germination

Hildebrand¹,

Hymowitz²

1981

Physiologia Plantarum

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Differences in starch metabolism during seed development and germination of two soybean [Glycine max (L.) Merrill] genotypes with normal seed β‐amylase activity [‘Williams’ (Sp1b and ‘Altona’ (Sp1b)] and two soybean genotypes with undetectable seed β‐amylase activity [‘Chestnut’ (Sp1au) and ‘Altona’ (Sp1)] were investigated. Starch and soluble sugar profiles were essentially the same during seed development and germination. Total amylase activity of Williams and Altona (Sp1b) peaked just prior to seed maturity and then dropped off slowly; whereas, the total amylase activity of Chestnut and Altona (sp1) was very low throughout seed development and germination. The differences in amylase activity between Altona (Sp 1 b) and Altona (sp 1) was also seen in leaves. α‐Amylase activity was similar in the four genotypes when β‐amylase was inhibited with Hg2+ but was higher in the two genotypes with normal β‐amylase activity when β‐amylase was inhibited with heat plus Ca2+. Low levels of starch phosphorylase activity were detected throughout seed development and germination, and the activity was similar in three of the genotypes and higher in Altona (sp 1). The protein, oil and oligosaccharide contents of mature seeds of the four genotypes were similar. Altona (sp 1 b) and (sp 1), which appear to be near isogenic lines, were not different in any morphological character or yield. Altona (Sp 1 b) showed greater hydrolysis of soybean seed starch than Altona (sp 1), but the evidence indicates that the mutation resulting in greatly reduced or missing β‐amylase activity has no effect on starch metabolism of developing and germinating soybean seeds.

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Soybean phosphatase. Purification and properties

Cited by 26 publications

References 9 publications

Characterization of Phytase of Beans (Phaseolus Vulgaris)

Characterization of Phytase of Beans (Phaseolus Vulgaris)

Survey of Microorganisms for the Production of Extracellular Phytase

Role of β‐amylase in starch metabolism during soybean seed development and germination

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