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PubMed1996

Purification, characterisation and steady state kinetic properties of cytosolic pyruvate kinase free of phosphoenol pyruvate phosphatase activity from germinating mung beans (Vigna radiata L.)

Mung bean pyruvate kinase (PK) practically free from PEP-phosphatase has been purified about 36 fold. The enzyme is irreversibly inactivated on desalting by gel filtration or dialysis (without EDTA). The inactivation is also observed in the presence of ATP, Mg2+ or thiols but is prevented by a non-proteinous, heat stable, small molecular mass factor present in the mung bean extract. Mung bean PK has a molecular mass of 210 kDa. It shows single exponential decay of activity at various temperatures (-4 to 60 degrees C). The Km of PEP and ADP are found to be 0.12 and 0.24 mM, respectively at pH 6.5, when the enzyme is saturated with the second substrate. The Km values for PEP and ADP are 0.05 and 0.16 mM, at pH 8.5 and 0.09 and 0.17 mM, respectively at pH 7.5. The optimum pH is 7.5. The enzyme shows an absolute requirement for Mg2+ (Km 0.43 mM) or Mn2+ ions (Km 0.125 mM). Potassium ions are not essential but activate the enzyme in the presence of Mg2+ or Mn2+ ions. ATP shows competitive inhibition with ADP and non-competitive with PEP. Kinetic studies at different pHs and effects of ATP suggest the formation of a ternary complex (E.ADP.PEP) by a combination of random and compulsory ordered pathways depending on the experimental conditions.

Acid Phosphatase↗
PubMed1996

Nutritional evaluation of a high-temperature dried soft wheat pasta supplemented with cowpea (Vigna unguiculata (L) Walp).

The objective of this study was to determine the nutritional quality of the pasta described above. The work was unique in the following aspects: 1) the drying process was a nonconventional method, consisting of a high-temperature short-time (HTST) process; 2) the nutritional quality of the wheat pasta was improved by the cowpea supplementation. Cowpea was especially chosen due to it being a staple food in the diet of the people in Northeast Brazil. Benefits attributed to the HTST drying process include a reduction in bacterial counts, shorter processing time and less energy consumption. In addition, there are reports in the literature of improved pasta firmness, color intensity, and cooking characteristics, when non Triticum durum materials plus drying are used. The pasta produced in this work was made using 100% soft wheat flour (SP), and soft wheat flour (SF) mixed supplemented with 10, 20 and 30% dehulled cowpea meal (CM); referred to as 10, 20 and 30% SP, respectively. The methods utilized in this project included: AACC methods for proximate analyses and trypsin inhibitor activity determination, atomic absorption spectrophotometry for mineral determination, a dye binding procedure for measuring available lysine, HPLC for amino acid quantification., FAO/WHO amino acid scoring patterns for chemical scores and AOAC for protein digestibility. The protein content of the past as supplemented with CM ranged from 11.3 to 14.2%, while the 100% SF pasta (SP) contained 10.9%. CM supplementation resulted in 52 to 113% more total lysine, and 26 to 82% more available lysine in the CM pasta compared to the SP. Chemical scores for SP were 45 and 59% for preschool and school-age children, respectively. Adding 30% CM to SP improved the above chemical scores to 89 and 100+, respectively. However, the addition of CM compromised the in vitro protein digestibility of SP from 4 to 6%. The addition fo 30% CM provided the SP with greater calcium (Ca), iron (Fe), zinc (Zn) and copper (Cu): 44, 49, 91 and 402% respectively. Cooking the CM pasta resulted in a 50 to 90% retention of mineral content, with the greatest loss being for Cu. In the cooked 30% CM pasta, the contents of Fe, Zn and Ca were, respectively, 50, 67 and 243% greater than their content in the cooked SP. Of the cooked pasta, the only one displaying trypsin inhibitor activity was the 30% CM pasta, which had 0.8 TIU.

Adult↗
PubMed1998

[Characterization of aldehyde dehydrogenase gene fragment from mung bean Vigna radiata using the polymerase chain reaction].

Two degenerate oligonucleotide sequence primers and polymerase chain reactions on total DNA have been utilized to clone on 651--bp gene fragment coding the central part of amino acid sequence of an earlier unknown aldehyde dehydrogenase (ALDH) from mung bean. The deduced partial amino acid sequence for this aldehyde dehydrogenase shows about 65% sequence identity to ALDHs of Vibrio cholerae Rhodococcus sp., Alcaligenes eutrophus and about 45% sequence identity to mammalian ALDHs 1 and 2, ALDHs of Aspergillus niger and A, nidulans, the betain aldehyde dehydrogenase from spinach. Alignment of the mung bean aldehyde dehydrogenase partial amino acid sequence with the sequence of 16 NAD(P)(+)-dependent aldehyde dehydrogenases has demonstrated that all strictly conserved amino acid residues and all three conservative regions are identical.

Aldehyde Dehydrogenase↗