A group from Max Planck Institute of Biophysics has simulated effects of ACE2 glycosylation onto binding to SARS-CoV-2 RBD.
https://www.pnas.org/content/118/19/e2100425118.long
Structurally speaking, there would be four glycosylation sites on ACE2 (N53, N90, N103, and N322）which have the possibility to interact with the RBD. The difference in glycan structures also affects binding strength to RBD, and asialo-types and high mannose show stronger interactions with the RBD at N70 and N322 positions. At the N90 position, high mannose has stronger affinity than asialo-types, and at the N322 position, vice versa.
Effects of glycans onto binding to RBD are different between N90 and N322 positions. The N90 glycan shields ACE2 from RBD binding, and the N322 glycan strengthens RBD binding, conversely. Actually, it has already reported that almost all mutations removing N322 glycosylation site are detrimental to the binding of the RBD. Since the N322 glycan interacts mainly with Y369–K378, R408, N437, N439, and V503 near the site of the N501Y mutation, it might be associated with increased ACE2 binding affinity and enhanced infectivity.
For your information, two articles related to effects of ACE2 glycosylation on to RBD binding have already introduced in this blog site.
The same thing has already demonstrated experimentally as sialic acids and high mannose weaken SARS-CoV-2 binding to ACE2.