Evidence map›Paper›PMID 33009584›Full record

ArticleApplied biochemistry and biotechnology2021

Exploring the Milk-Clotting and Proteolytic Activities in Different Tissues of Vallesia glabra: a New Source of Plant Proteolytic Enzymes.

Daniel A González-Velázquez, Miguel A Mazorra-Manzano, Marcel Martínez-Porchas, José A Huerta-Ocampo, Belinda Vallejo-Córdoba, Wendy G Mora-Cortes, Jesús M Moreno-Hernández, Juan C Ramírez-Suarez

Abstract read
PubMed Publisher
In one paragraph

Article in Applied biochemistry and biotechnology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.9field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

6 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Plant Milk-Clotting Enzymes for Cheesemaking.Foods (Basel, Switzerland) · 2022
    Review
  5. Article
  6. Hemoglobin Precipitation: An Index ofEvidence-based complementary and alternative medicine : eCAM · 2021
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

Daniel A González-VelázquezCoordinación de Tecnología de Alimentos de Origen Animal, Laboratorio de Química de Alimentos y Biotecnología de Productos Lácteos, Centro de Investigación en Alimentación y Desarrollo, A.C, Carretera Gustavo Enrique Astiazarán Rosas No. 46, Colonia La Victoria, CP. 83304, Hermosillo, Sonora, Mexico.
Miguel A Mazorra-ManzanoCoordinación de Tecnología de Alimentos de Origen Animal, Laboratorio de Química de Alimentos y Biotecnología de Productos Lácteos, Centro de Investigación en Alimentación y Desarrollo, A.C, Carretera Gustavo Enrique Astiazarán Rosas No. 46, Colonia La Victoria, CP. 83304, Hermosillo, Sonora, Mexico. mazorra@ciad.mx.ORCID http://orcid.org/0000-0002-1425-4250
Marcel Martínez-PorchasCoordinación de Tecnología de Alimentos de Origen Animal, Laboratorio de Biología de Organismos Acuáticos, Centro de Investigación en Alimentación y Desarrollo, A.C., Gustavo Enrique Astiazarán Rosas No. 46, Colonia La Victoria, CP. 83304, Hermosillo, Sonora, Mexico.
José A Huerta-OcampoLaboratorio de Bioquímica de Proteínas y Glicanos. Carretera, CONACYT-Centro de Investigación en Alimentación y Desarrollo A.C., Gustavo Enrique Astiazarán Rosas No. 46, Colonia La Victoria, CP. 83304, Hermosillo, Sonora, Mexico.
Belinda Vallejo-CórdobaCoordinación de Tecnología de Alimentos de Origen Animal, Laboratorio de Química de Alimentos y Biotecnología de Productos Lácteos, Centro de Investigación en Alimentación y Desarrollo, A.C, Carretera Gustavo Enrique Astiazarán Rosas No. 46, Colonia La Victoria, CP. 83304, Hermosillo, Sonora, Mexico.
Wendy G Mora-CortesCoordinación de Tecnología de Alimentos de Origen Animal, Laboratorio de Química de Alimentos y Biotecnología de Productos Lácteos, Centro de Investigación en Alimentación y Desarrollo, A.C, Carretera Gustavo Enrique Astiazarán Rosas No. 46, Colonia La Victoria, CP. 83304, Hermosillo, Sonora, Mexico.
Jesús M Moreno-HernándezInstituto Nacional de Investigaciones Forestales, Agrícolas y Pecuarias (INIFAP), Carretera Culiacán-Eldorado km 17,5, Culiacán, Sinaloa, Mexico.
Juan C Ramírez-SuarezCoordinación de Tecnología de Alimentos de Origen Animal, Laboratorio de Bioquímica y Calidad de Productos Pesqueros, Centro de Investigación en Alimentación y Desarrollo, A.C, Carretera. Gustavo Enrique Astiazarán Rosas No. 46, Colonia La Victoria, C.P. 83304, Hermosillo, Sonora, Mexico.
Centro de Investigación en Alimentación y Desarrollo · MXInstituto Nacional de Investigaciones Forestales Agrícolas y Pecuarias · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteolytic enzymes are widely distributed in nature, playing essential roles in important biological functions. Recently, the use of plant proteases at the industrial level has mainly increased in the food industry (e.g., cheesemaking, meat tenderizing, and protein hydrolysate production). Current technological and scientific advances in the detection and characterization of proteolytic enzymes have encouraged the search for new natural sources. Thus, this work aimed to explore the milk-clotting and proteolytic properties of different tissues of Vallesia glabra. Aqueous extracts from the leaves, fruits, and seeds of V. glabra presented different protein profiles, proteolytic activity, and milk-clotting activity. The milk-clotting activity increased with temperature (30-65 °C), but this activity was higher in leaf (0.20 MCU/mL) compared with that in fruit and seed extracts (0.12 and 0.11 MCU/mL, respectively) at 50 °C. Proteolytic activity in the extracts assayed at different pH (2.5-12.0) suggested the presence of different types of active proteases, with maximum activity at acidic conditions (4.0-4.5). Inhibitory studies indicated that major activity in V. glabra extracts is related to cysteine proteases; however, the presence of serine, aspartic, and metalloproteases was also evident. The hydrolytic profile of caseins indicated that V. glabra leaves could be used as a rennet substitute in cheesemaking, representing a new and promising source of proteolytic enzymes.

Indexed as

ProteolysisAnimalsApocynaceaeHydrogen-Ion ConcentrationMilkPeptide HydrolasesPlant LeavesPlant ProteinsSeedsPeptide HydrolasesPlant ProteinsMilk-clottingPlant tissuesProteolytic enzymesVallesia glabraZymography

Identifiers

PMID33009584
OpenAlexW3090891666

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.