Homology Modeling and Analysis of Vacuolar Aspartyl Protease from a Novel Yeast Expression Host Meyerozyma guilliermondii Strain SO
Author:
Funder
Ministry of Higher Education, Malaysia
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
https://link.springer.com/content/pdf/10.1007/s13369-022-07153-1.pdf
Reference70 articles.
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2. Stanforth, K.J.; Wilcox, M.D.; Chater, P.I.; Brownlee, I.A.; Zakhour, M.I.; Banecki, K.M.R.M.; Pearson, J.P.: Pepsin properties, structure, and its accurate measurement: a narrative review. Ann. Esophagus (2021). https://doi.org/10.21037/aoe-20-95
3. Yegin, S.; Dekker, P.: Progress in the field of aspartic proteinases in cheese manufacturing: structures, functions, catalytic mechanism, inhibition and engineering. Dairy Sci. Technol. 93, 565–594 (2013). https://doi.org/10.1007/s13594-013-0137-2
4. Hsiao, N.W.; Chen, Y.; Kuan, Y.C.; Lee, S.K.; Chan, H.H.; Kao, C.H.: Purification and characterization of aspartic protease from the Rhizopus oryzae protease extract, Peptidase R. Electron J. Biotechnol. 17, 89–94 (2014). https://doi.org/10.1016/j.ejbt.2014.02.002
5. Minina, E.A.; Moschou, P.N.; Bozhkov, P.V.: Limited and digestive proteolysis: crosstalk between evolutionary conserved pathways. New Phytol. 215, 958–964 (2017)
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