Abstract
An amylase from alfalfa (Medicago sativa L. c.v. Moapa) seeds was purified by column chromatography and gel filtration, followed by chromatofocusing on Mono P HR 5/20. The last step was effective for separation of the alfalfa amylase to a homogeneous state. The purified amylase was identified as beta-amylase from the fact that only beta-maltose was formed by the enzymatic degradation of soluble starch. The molecular weight and specific activity of the beta-amylase (E1%(280 nm) = 18.3) were determined to be 61,000 and 1,077 A.U./mg, respectively. The beta-amylase activity was inhibited by the modification of sulfhydryl groups with p-chloromercuribenzoic acid. The optimum pH and isoelectric point of alfalfa beta-amylase were 7.0 and 4.8, respectively, which were different from other plant beta-amylases.
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Claims 7
Claim · model-written summary
Chromatofocusing separated alfalfa amylase to a homogeneous state.
- Taxon
- alfalfa
Medicago sativae0 - Outcome
- separation of the alfalfa amylase to a homogeneous statee0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The last step was effective for separation of the alfalfa amylase to a homogeneous state.”
Claim · model-written summary
Purified alfalfa amylase was identified as beta-amylase because soluble starch degradation formed only beta-maltose.
- Taxon
- AlfalfaMedicago sativat0
- Gene
- beta-amylasee0
- Outcome
- only beta-maltose was formede0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The purified amylase was identified as beta-amylase from the fact that only beta-maltose was formed by the enzymatic degradation of soluble starch.”
t0“Alfalfa”
Claim · model-written summary
Alfalfa beta-amylase had molecular weight 61,000.
- Taxon
- AlfalfaMedicago sativat0
- Gene
- beta-amylasee0
- Outcome
- molecular weighte0
- Value
- 61,000e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The molecular weight and specific activity of the beta-amylase (E1%(280 nm) = 18.3) were determined to be 61,000 and 1,077 A.U./mg, respectively.”
t0“Alfalfa”
Claim · model-written summary
Alfalfa beta-amylase had specific activity 1,077 A.U./mg.
- Taxon
- AlfalfaMedicago sativat0
- Gene
- beta-amylasee0
- Outcome
- specific activitye0
- Value
- 1,077 A.U./mge0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The molecular weight and specific activity of the beta-amylase (E1%(280 nm) = 18.3) were determined to be 61,000 and 1,077 A.U./mg, respectively.”
t0“Alfalfa”
Claim · model-written summary
Modification of sulfhydryl groups with p-chloromercuribenzoic acid inhibited alfalfa beta-amylase activity.
- Taxon
- AlfalfaMedicago sativat0
- Treatment
- modification of sulfhydryl groups with p-chloromercuribenzoic acide0
- Outcome
- beta-amylase activitye0
- Direction
- inhibitede0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The beta-amylase activity was inhibited by the modification of sulfhydryl groups with p-chloromercuribenzoic acid.”
t0“Alfalfa”
Claim · model-written summary
Alfalfa beta-amylase had optimum pH 7.0.
- Taxon
- alfalfaMedicago sativae0
- Gene
- beta-amylasee0
- Outcome
- optimum pHe0
- Value
- 7.0e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The optimum pH and isoelectric point of alfalfa beta-amylase were 7.0 and 4.8, respectively, which were different from other plant beta-amylases.”
Claim · model-written summary
Alfalfa beta-amylase had isoelectric point 4.8.
- Taxon
- alfalfaMedicago sativae0
- Gene
- beta-amylasee0
- Outcome
- isoelectric pointe0
- Value
- 4.8e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“The optimum pH and isoelectric point of alfalfa beta-amylase were 7.0 and 4.8, respectively, which were different from other plant beta-amylases.”