A soybean vacuolar protein (P34) related to thiol proteases is synthesized as a glycoprotein precursor during seed maturation.

Kaliński, A.; Melroy, Daine L.; Dwivedi, Radhey Shyam; Herman, Eliot M.

doi:10.1016/s0021-9258(19)49807-4

Cited by 104 publications

(28 citation statements)

References 48 publications

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“…Compared with these thiol proteases, a Gly37 replaced the conserved catalytic Cys in P34; of the three SS, two were present in P34 (Cys68-Cys108 and Cys171-Cys224, Figure ). However, one of the three SS in other thiol proteases existed as Cys34 and Asn77 in P34, so it was suggested that the Cys34 near Gly37 might be a free thiol and acted as the active-site residue. , 30K, an allergenic protein, was first identified by Ogawa et al, , and considered as a similar protein to P34 owing to their similar amino acid compositions. However, the Arg46, Ser75, Gln80, and Phe203 of P34 were replaced by the Ser46, Cys75, His80, and Glu203 of 30K (Figure ).…”

Section: Introductionmentioning

confidence: 99%

Soybean P34 Probable Thiol Protease Probably Has Proteolytic Activity on Oleosins

Zhao

Kong

Zhang

et al. 2017

J. Agric. Food Chem.

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P34 probable thiol protease (P34) and Gly m Bd 30K (30K) show high relationship with the protease of 24 kDa oleosin of soybean oil bodies. In this study, 9 day germinated soybean was used to separate bioprocessed P34 (P32) from bioprocessed 30K (28K). Interestingly, P32 existed as dimer, whereas 28K existed as monomer; a P32-rich sample had proteolytic activity and high cleavage site specificity (Lys-Thr of 24 kDa oleosin), whereas a 28K-rich sample showed low proteolytic activity; the P32-rich sample contained one thiol protease. After mixing with purified oil bodies, all P32 dimers were dissociated and bound to 24 kDa oleosins to form P32-24 kDa oleosin complexes. By incubation, 24 kDa oleosin was preferentially hydrolyzed, and two hydrolyzed products (HPs; 17 and 7 kDa) were confirmed. After most of 24 kDa oleosin was hydrolyzed, some P32 existed as dimer, and the other as P32-17 kDa HP. It was suggested that P32 was the protease.

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Section: Introductionmentioning

confidence: 99%

Soybean P34 Probable Thiol Protease Probably Has Proteolytic Activity on Oleosins

Zhao

Kong

Zhang

et al. 2017

J. Agric. Food Chem.

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“…In the first research about soybean OB oleosin, P34, a protein comprised of 257 amino acid residues (AARs), was wrongly considered as one kind of oleosin . In two later researches, , it was found that P34, having considerable sequence similarity to the thiol proteases of papain family, originated from pro-P34 (47 kDa) during seed maturation and stored in protein storage vacuoles (PSVs). Different from P34, many other seed thiol proteases, which are closely correlated with storage protein mobilization, are synthesized only after seed germination, , revealing that P34 may possess different biological activity.…”

Section: Introductionmentioning

confidence: 99%

“…In two later researches, , it was found that P34, having considerable sequence similarity to the thiol proteases of papain family, originated from pro-P34 (47 kDa) during seed maturation and stored in protein storage vacuoles (PSVs). Different from P34, many other seed thiol proteases, which are closely correlated with storage protein mobilization, are synthesized only after seed germination, , revealing that P34 may possess different biological activity. Structurally, the thiol proteases of the papain family possessed highly conserved catalytic triad (Cys-His-Asn) residues and three disulfide bonds .…”

Section: Introductionmentioning

confidence: 99%

Oleosins (24 and 18 kDa) Are Hydrolyzed Not Only in Extracted Soybean Oil Bodies but Also in Soybean Germination

Zhao

Cao

Kong

et al. 2014

J. Agric. Food Chem.

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After oil bodies (OBs) were extracted from ungerminated soybean by pH 6.8 extraction, it was found that 24 and 18 kDa oleosins were hydrolyzed in the extracted OBs, which contained many OB extrinsic proteins (i.e., lipoxygenase, β-conglycinin, γ-conglycinin, β-amylase, glycinin, Gly m Bd 30K (Bd 30K), and P34 probable thiol protease (P34)) as well as OB intrinsic proteins. In this study, some properties (specificity, optimal pH and temperature) of the proteases of 24 and 18 kDa oleosins and the oleosin hydrolysis in soybean germination were examined, and the high relationship between Bd 30K/P34 and the proteases was also discussed. The results showed (1) the proteases were OB extrinsic proteins, which had high specificity to hydrolyze 24 and 18 kDa oleosins, and cleaved the specific peptide bonds to form limited hydrolyzed products; (2) 24 and 18 kDa oleosins were not hydrolyzed in the absence of Bd 30K and P34 (or some Tricine-SDS-PAGE undetectable proteins); (3) the protease of 24 kDa oleosin had strong resistance to alkaline pH while that of 18 kDa oleosin had weak resistance to alkaline pH, and Bd 30K and P34, resolved into two spots on two-dimensional electrophoresis gel, also showed the same trend; (4) 16 kDa oleosin as well as 24 and 18 kDa oleosins were hydrolyzed in soybean germination, and Bd 30K and P34 were always contained in the extracted OBs from germinated soybean even when all oleosins were hydrolyzed; (5) the optimal temperature and pH of the proteases were respectively determined as in the ranges of 35-50 °C and pH 6.0-6.5, while 60 °C or pH 11.0 could denature them.

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“… 26–28 The proteins with a molecular weight of 17 kDa, 18 kDa and 24 kDa are the soybean oleosin proteins, while the protein with a molecular weight of 34 kDa is present in the vacuoles of the plant seed storage protein because it can be tightly integrated with the soybean oil body and is initially considered to be a soybean oil body protein. 27,28 After the soybean oil bodies were washed with Tris–HCl buffer solution, background proteins were partially removed (β-conglycinin, glycinin, etc. ) (Lane 2, Fig.…”

Section: Resultsmentioning

confidence: 99%

Effect of sodium alginate on the stability of natural soybean oil body emulsions

Feng

et al. 2018

RSC Adv.

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A soybean vacuolar protein (P34) related to thiol proteases is synthesized as a glycoprotein precursor during seed maturation.

Cited by 104 publications

References 48 publications

Soybean P34 Probable Thiol Protease Probably Has Proteolytic Activity on Oleosins

Soybean P34 Probable Thiol Protease Probably Has Proteolytic Activity on Oleosins

Oleosins (24 and 18 kDa) Are Hydrolyzed Not Only in Extracted Soybean Oil Bodies but Also in Soybean Germination

Effect of sodium alginate on the stability of natural soybean oil body emulsions

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